STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY
REINEMER P, GRAMS F, HUBER R, KLEINE T, SCHNIERER S, PIPER M, Tschesche H, BODE W (1994)
FEBS LETTERS 338(2): 227-233.
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Autor*in
REINEMER, P;
GRAMS, F;
HUBER, R;
KLEINE, T;
SCHNIERER, S;
PIPER, M;
Tschesche, HaraldUniBi;
BODE, W
Einrichtung
Abstract / Bemerkung
For the collagenases PMNL-CL and FIB-CL, the presence of the N-terminal Phe(79) correlates with an increase in proteolytic activity. We have determined the X-ray crystal structure of the recombinant Phe(79)-Gly(242) Catalytic domain of human neutrophil collagenase (PMNL-CL, MMP-8) using the recently solved model of the Met(80)-Gly(242) form for phasing and subsequently refined it to a final crystalographic R-factor of 18.0% at 2.5 Angstrom resolution. The PMNL-CL catalytic domain is a spherical molecule with a flat active site cleft separating a smaller C-terminal subdomain from a bigger N-terminal domain, that harbours two zinc ions, namely a 'structural' and a 'catalytic' zinc, and two calcium ions. The N-terminal segment prior to Pro(86), which is disordered in the Met(80)-Gly(242) form, packs against a concave hydrophobic surface made by the C-terminal helix. The N-terminal Phe(79) ammonium group makes a salt link with the side chain carboxylate group of the strictly conserved Asp(232). Stabilization of the catalytic site might be conferred via strong hydrogen bonds made by the adjacent, likewise strictly conserved Asp(233) With the characteristic 'Met-turn', which forms the base of the active site residues.
Stichworte
COLLAGENASE;
MATRIX METALLOPROTEINASE;
ZINC ENDOPEPTIDASE FAMILY;
X-RAY;
CRYSTAL STRUCTURE;
SUPERACTIVATION
Erscheinungsjahr
1994
Zeitschriftentitel
FEBS LETTERS
Band
338
Ausgabe
2
Seite(n)
227-233
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1644336
Zitieren
REINEMER P, GRAMS F, HUBER R, et al. STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY. FEBS LETTERS. 1994;338(2):227-233.
REINEMER, P., GRAMS, F., HUBER, R., KLEINE, T., SCHNIERER, S., PIPER, M., Tschesche, H., et al. (1994). STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY. FEBS LETTERS, 338(2), 227-233. https://doi.org/10.1016/0014-5793(94)80370-6
REINEMER, P, GRAMS, F, HUBER, R, KLEINE, T, SCHNIERER, S, PIPER, M, Tschesche, Harald, and BODE, W. 1994. “STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY”. FEBS LETTERS 338 (2): 227-233.
REINEMER, P., GRAMS, F., HUBER, R., KLEINE, T., SCHNIERER, S., PIPER, M., Tschesche, H., and BODE, W. (1994). STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY. FEBS LETTERS 338, 227-233.
REINEMER, P., et al., 1994. STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY. FEBS LETTERS, 338(2), p 227-233.
P. REINEMER, et al., “STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY”, FEBS LETTERS, vol. 338, 1994, pp. 227-233.
REINEMER, P., GRAMS, F., HUBER, R., KLEINE, T., SCHNIERER, S., PIPER, M., Tschesche, H., BODE, W.: STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY. FEBS LETTERS. 338, 227-233 (1994).
REINEMER, P, GRAMS, F, HUBER, R, KLEINE, T, SCHNIERER, S, PIPER, M, Tschesche, Harald, and BODE, W. “STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE SUPERACTIVATION OF COLLAGENASES - A CRYSTALLOGRAPHIC STUDY”. FEBS LETTERS 338.2 (1994): 227-233.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
PDB
1 Eintrag gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 1jan)
Protein structure name: complex of pro-leu-gly-hydroxylamine with the catalytic domain of matrix metallo proteinase-8 (phe79 form)
Public wwPDB file in PDB format
Protein structure name: complex of pro-leu-gly-hydroxylamine with the catalytic domain of matrix metallo proteinase-8 (phe79 form)
Public wwPDB file in PDB format
UNIPROT
1 Eintrag gefunden, die diesen Artikel zitieren
63 Zitationen in Europe PMC
Daten bereitgestellt von Europe PubMed Central.
A novel mechanism of latency in matrix metalloproteinases.
López-Pelegrín M, Ksiazek M, Karim AY, Guevara T, Arolas JL, Potempa J, Gomis-Rüth FX., J Biol Chem 290(8), 2015
PMID: 25555916
López-Pelegrín M, Ksiazek M, Karim AY, Guevara T, Arolas JL, Potempa J, Gomis-Rüth FX., J Biol Chem 290(8), 2015
PMID: 25555916
Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.
Stura EA, Visse R, Cuniasse P, Dive V, Nagase H., FASEB J 27(11), 2013
PMID: 23913860
Stura EA, Visse R, Cuniasse P, Dive V, Nagase H., FASEB J 27(11), 2013
PMID: 23913860
Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemokine and vimentin cleavages enhance cell migration and macrophage phagocytic activities.
Starr AE, Bellac CL, Dufour A, Goebeler V, Overall CM., J Biol Chem 287(16), 2012
PMID: 22367194
Starr AE, Bellac CL, Dufour A, Goebeler V, Overall CM., J Biol Chem 287(16), 2012
PMID: 22367194
The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases.
Cerdà-Costa N, Guevara T, Karim AY, Ksiazek M, Nguyen KA, Arolas JL, Potempa J, Gomis-Rüth FX., Mol Microbiol 79(1), 2011
PMID: 21166898
Cerdà-Costa N, Guevara T, Karim AY, Ksiazek M, Nguyen KA, Arolas JL, Potempa J, Gomis-Rüth FX., Mol Microbiol 79(1), 2011
PMID: 21166898
Proenzyme structure and activation of astacin metallopeptidase.
Guevara T, Yiallouros I, Kappelhoff R, Bissdorf S, Stöcker W, Gomis-Rüth FX., J Biol Chem 285(18), 2010
PMID: 20202938
Guevara T, Yiallouros I, Kappelhoff R, Bissdorf S, Stöcker W, Gomis-Rüth FX., J Biol Chem 285(18), 2010
PMID: 20202938
Molecular dynamics simulations of the active matrix metalloproteinase-2: positioning of the N-terminal fragment and binding of a small peptide substrate.
Díaz N, Suárez D., Proteins 72(1), 2008
PMID: 18186480
Díaz N, Suárez D., Proteins 72(1), 2008
PMID: 18186480
Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-2.
Maskos K, Lang R, Tschesche H, Bode W., J Mol Biol 366(4), 2007
PMID: 17196980
Maskos K, Lang R, Tschesche H, Bode W., J Mol Biol 366(4), 2007
PMID: 17196980
Crystal structures of MMP-9 complexes with five inhibitors: contribution of the flexible Arg424 side-chain to selectivity.
Tochowicz A, Maskos K, Huber R, Oltenfreiter R, Dive V, Yiotakis A, Zanda M, Pourmotabbed T, Bode W, Goettig P., J Mol Biol 371(4), 2007
PMID: 17599356
Tochowicz A, Maskos K, Huber R, Oltenfreiter R, Dive V, Yiotakis A, Zanda M, Pourmotabbed T, Bode W, Goettig P., J Mol Biol 371(4), 2007
PMID: 17599356
Crystal structure of an active form of human MMP-1.
Iyer S, Visse R, Nagase H, Acharya KR., J Mol Biol 362(1), 2006
PMID: 16890240
Iyer S, Visse R, Nagase H, Acharya KR., J Mol Biol 362(1), 2006
PMID: 16890240
Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs.
Cuniasse P, Devel L, Makaritis A, Beau F, Georgiadis D, Matziari M, Yiotakis A, Dive V., Biochimie 87(3-4), 2005
PMID: 15781327
Cuniasse P, Devel L, Makaritis A, Beau F, Georgiadis D, Matziari M, Yiotakis A, Dive V., Biochimie 87(3-4), 2005
PMID: 15781327
Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features.
Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K., J Mol Biol 336(1), 2004
PMID: 14741217
Lang R, Braun M, Sounni NE, Noel A, Frankenne F, Foidart JM, Bode W, Maskos K., J Mol Biol 336(1), 2004
PMID: 14741217
Structural basis of the matrix metalloproteinases and their physiological inhibitors, the tissue inhibitors of metalloproteinases.
Bode W, Maskos K., Biol Chem 384(6), 2003
PMID: 12887053
Bode W, Maskos K., Biol Chem 384(6), 2003
PMID: 12887053
Structural aspects of the metzincin clan of metalloendopeptidases.
Gomis-Rüth FX., Mol Biotechnol 24(2), 2003
PMID: 12746556
Gomis-Rüth FX., Mol Biotechnol 24(2), 2003
PMID: 12746556
Screening of stress enhancer based on analysis of gene expression profiles: enhancement of hyperthermia-induced tumor necrosis by an MMP-3 inhibitor.
Kato N, Kobayashi T, Honda H., Cancer Sci 94(7), 2003
PMID: 12841876
Kato N, Kobayashi T, Honda H., Cancer Sci 94(7), 2003
PMID: 12841876
Modeling of enzyme-substrate complexes for the metalloproteases MMP-3, ADAM-9 and ADAM-10.
Manzetti S, McCulloch DR, Herington AC, van der Spoel D., J Comput Aided Mol Des 17(9), 2003
PMID: 14713188
Manzetti S, McCulloch DR, Herington AC, van der Spoel D., J Comput Aided Mol Des 17(9), 2003
PMID: 14713188
Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases.
Maskos K, Bode W., Mol Biotechnol 25(3), 2003
PMID: 14668538
Maskos K, Bode W., Mol Biotechnol 25(3), 2003
PMID: 14668538
Computational study of the catalytic domain of human neutrophil collagenase. specific role of the S3 and S'3 subsites in the interaction with a phosphonate inhibitor.
Aschi M, Roccatano D, Di Nola A, Gallina C, Gavuzzo E, Pochetti G, Pieper M, Tschesche H, Mazza F., J Comput Aided Mol Des 16(3), 2002
PMID: 12363219
Aschi M, Roccatano D, Di Nola A, Gallina C, Gavuzzo E, Pochetti G, Pieper M, Tschesche H, Mazza F., J Comput Aided Mol Des 16(3), 2002
PMID: 12363219
Protease inhibitors: synthesis of matrix metalloproteinase and bacterial collagenase inhibitors incorporating 5-amino-2-mercapto-1,3,4-thiadiazole zinc binding functions.
Scozzafava A, Supuran CT., Bioorg Med Chem Lett 12(19), 2002
PMID: 12217351
Scozzafava A, Supuran CT., Bioorg Med Chem Lett 12(19), 2002
PMID: 12217351
Tetrahydroisoquinoline-3-carboxylate based matrix-metalloproteinase inhibitors: design, synthesis and structure-activity relationship.
Matter H, Schudok M, Schwab W, Thorwart W, Barbier D, Billen G, Haase B, Neises B, Weithmann K, Wollmann T., Bioorg Med Chem 10(11), 2002
PMID: 12213468
Matter H, Schudok M, Schwab W, Thorwart W, Barbier D, Billen G, Haase B, Neises B, Weithmann K, Wollmann T., Bioorg Med Chem 10(11), 2002
PMID: 12213468
The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition.
Brandstetter H, Grams F, Glitz D, Lang A, Huber R, Bode W, Krell HW, Engh RA., J Biol Chem 276(20), 2001
PMID: 11278347
Brandstetter H, Grams F, Glitz D, Lang A, Huber R, Bode W, Krell HW, Engh RA., J Biol Chem 276(20), 2001
PMID: 11278347
Pyrimidine-2,4,6-Triones: a new effective and selective class of matrix metalloproteinase inhibitors.
Grams F, Brandstetter H, D'Alò S, Geppert D, Krell HW, Leinert H, Livi V, Menta E, Oliva A, Zimmermann G, Gram F, Brandstetter H, D'Alò S, Geppert D, Krell HW, Leinert H, Livi VMenta E, Oliva A, Zimmermann G., Biol Chem 382(8), 2001
PMID: 11592410
Grams F, Brandstetter H, D'Alò S, Geppert D, Krell HW, Leinert H, Livi V, Menta E, Oliva A, Zimmermann G, Gram F, Brandstetter H, D'Alò S, Geppert D, Krell HW, Leinert H, Livi VMenta E, Oliva A, Zimmermann G., Biol Chem 382(8), 2001
PMID: 11592410
Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure.
Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K., J Mol Biol 312(4), 2001
PMID: 11575928
Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K., J Mol Biol 312(4), 2001
PMID: 11575928
Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor.
Nar H, Werle K, Bauer MM, Dollinger H, Jung B., J Mol Biol 312(4), 2001
PMID: 11575929
Nar H, Werle K, Bauer MM, Dollinger H, Jung B., J Mol Biol 312(4), 2001
PMID: 11575929
Design and synthesis of carboxylate inhibitors for matrix metalloproteinases.
Fujisawa T, Katakura S, Odake S, Morita Y, Yasuda J, Yasumatsu I, Morikawa T., Chem Pharm Bull (Tokyo) 49(10), 2001
PMID: 11605653
Fujisawa T, Katakura S, Odake S, Morita Y, Yasuda J, Yasumatsu I, Morikawa T., Chem Pharm Bull (Tokyo) 49(10), 2001
PMID: 11605653
The conserved methionine residue of the metzincins: a site-directed mutagenesis study.
Hege T, Baumann U., J Mol Biol 314(2), 2001
PMID: 11718552
Hege T, Baumann U., J Mol Biol 314(2), 2001
PMID: 11718552
A rationalization of the acidic pH dependence for stromelysin-1 (Matrix metalloproteinase-3) catalysis and inhibition.
Johnson LL, Pavlovsky AG, Johnson AR, Janowicz JA, Man CF, Ortwine DF, Purchase CF, White AD, Hupe DJ., J Biol Chem 275(15), 2000
PMID: 10753905
Johnson LL, Pavlovsky AG, Johnson AR, Janowicz JA, Man CF, Ortwine DF, Purchase CF, White AD, Hupe DJ., J Biol Chem 275(15), 2000
PMID: 10753905
Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes.
Terp GE, Christensen IT, Jørgensen FS., J Biomol Struct Dyn 17(6), 2000
PMID: 10949161
Terp GE, Christensen IT, Jørgensen FS., J Biomol Struct Dyn 17(6), 2000
PMID: 10949161
Identification of metal ligands in the Clostridium histolyticum ColH collagenase.
Jung CM, Matsushita O, Katayama S, Minami J, Sakurai J, Okabe A., J Bacteriol 181(9), 1999
PMID: 10217773
Jung CM, Matsushita O, Katayama S, Minami J, Sakurai J, Okabe A., J Bacteriol 181(9), 1999
PMID: 10217773
Specificity of inhibition of matrix metalloproteinase activity by doxycycline: relationship to structure of the enzyme.
Smith GN, Mickler EA, Hasty KA, Brandt KD., Arthritis Rheum 42(6), 1999
PMID: 10366106
Smith GN, Mickler EA, Hasty KA, Brandt KD., Arthritis Rheum 42(6), 1999
PMID: 10366106
Insights into MMP-TIMP interactions.
Bode W, Fernandez-Catalan C, Grams F, Gomis-Rüth FX, Nagase H, Tschesche H, Maskos K., Ann N Y Acad Sci 878(), 1999
PMID: 10415721
Bode W, Fernandez-Catalan C, Grams F, Gomis-Rüth FX, Nagase H, Tschesche H, Maskos K., Ann N Y Acad Sci 878(), 1999
PMID: 10415721
The second type II module from human matrix metalloproteinase 2: structure, function and dynamics.
Briknarová K, Grishaev A, Bányai L, Tordai H, Patthy L, Llinás M., Structure 7(10), 1999
PMID: 10545322
Briknarová K, Grishaev A, Bányai L, Tordai H, Patthy L, Llinás M., Structure 7(10), 1999
PMID: 10545322
Matrix metalloproteases: variations on a theme.
Borkakoti N., Prog Biophys Mol Biol 70(1), 1998
PMID: 9785958
Borkakoti N., Prog Biophys Mol Biol 70(1), 1998
PMID: 9785958
Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
Khan AR, James MN., Protein Sci 7(4), 1998
PMID: 9568890
Khan AR, James MN., Protein Sci 7(4), 1998
PMID: 9568890
Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F., Protein Sci 7(6), 1998
PMID: 9655333
Brandstetter H, Engh RA, Von Roedern EG, Moroder L, Huber R, Bode W, Grams F., Protein Sci 7(6), 1998
PMID: 9655333
Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K., EMBO J 17(17), 1998
PMID: 9724659
Fernandez-Catalan C, Bode W, Huber R, Turk D, Calvete JJ, Lichte A, Tschesche H, Maskos K., EMBO J 17(17), 1998
PMID: 9724659
Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus.
Gong W, Zhu X, Liu S, Teng M, Niu L., J Mol Biol 283(3), 1998
PMID: 9784374
Gong W, Zhu X, Liu S, Teng M, Niu L., J Mol Biol 283(3), 1998
PMID: 9784374
Solution structures of stromelysin complexed to thiadiazole inhibitors.
Stockman BJ, Waldon DJ, Gates JA, Scahill TA, Kloosterman DA, Mizsak SA, Jacobsen EJ, Belonga KL, Mitchell MA, Mao B, Petke JD, Goodman L, Powers EA, Ledbetter SR, Kaytes PS, Vogeli G, Marshall VP, Petzold GL, Poorman RA., Protein Sci 7(11), 1998
PMID: 9827994
Stockman BJ, Waldon DJ, Gates JA, Scahill TA, Kloosterman DA, Mizsak SA, Jacobsen EJ, Belonga KL, Mitchell MA, Mao B, Petke JD, Goodman L, Powers EA, Ledbetter SR, Kaytes PS, Vogeli G, Marshall VP, Petzold GL, Poorman RA., Protein Sci 7(11), 1998
PMID: 9827994
Assignments and structure determination of the catalytic domain of human fibroblast collagenase using 3D double and triple resonance NMR spectroscopy.
McCoy MA, Dellwo MJ, Schneider DM, Banks TM, Falvo J, Vavra KJ, Mathiowetz AM, Qoronfleh MW, Ciccarelli R, Cook ER, Pulvino TA, Wahl RC, Wang H., J Biomol NMR 9(1), 1997
PMID: 9081540
McCoy MA, Dellwo MJ, Schneider DM, Banks TM, Falvo J, Vavra KJ, Mathiowetz AM, Qoronfleh MW, Ciccarelli R, Cook ER, Pulvino TA, Wahl RC, Wang H., J Biomol NMR 9(1), 1997
PMID: 9081540
Relating matrix metalloproteinase structure to function: why the "hemopexin" domain?
Murphy G, Knäuper V., Matrix Biol 15(8-9), 1997
PMID: 9138283
Murphy G, Knäuper V., Matrix Biol 15(8-9), 1997
PMID: 9138283
The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.
Baumeister W, Cejka Z, Kania M, Seemüller E., Biol Chem 378(3-4), 1997
PMID: 9165062
Baumeister W, Cejka Z, Kania M, Seemüller E., Biol Chem 378(3-4), 1997
PMID: 9165062
Stromelysin-3: a paradigm for stroma-derived factors implicated in carcinoma progression.
Basset P, Bellocq JP, Lefebvre O, Noël A, Chenard MP, Wolf C, Anglard P, Rio MC., Crit Rev Oncol Hematol 26(1), 1997
PMID: 9246540
Basset P, Bellocq JP, Lefebvre O, Noël A, Chenard MP, Wolf C, Anglard P, Rio MC., Crit Rev Oncol Hematol 26(1), 1997
PMID: 9246540
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile.
Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Rüth FX., Eur J Biochem 247(1), 1997
PMID: 9249047
Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Rüth FX., Eur J Biochem 247(1), 1997
PMID: 9249047
Activation of human neutrophil procollagenase by stromelysin 2.
Knäuper V, Murphy G, Tschesche H., Eur J Biochem 235(1-2), 1996
PMID: 8631328
Knäuper V, Murphy G, Tschesche H., Eur J Biochem 235(1-2), 1996
PMID: 8631328
Human matrix metalloproteinase specificity studies using collagen sequence-based synthetic peptides.
Nagase H, Fields GB., Biopolymers 40(4), 1996
PMID: 8765610
Nagase H, Fields GB., Biopolymers 40(4), 1996
PMID: 8765610
Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage.
Mitchell PG, Magna HA, Reeves LM, Lopresti-Morrow LL, Yocum SA, Rosner PJ, Geoghegan KF, Hambor JE., J Clin Invest 97(3), 1996
PMID: 8609233
Mitchell PG, Magna HA, Reeves LM, Lopresti-Morrow LL, Yocum SA, Rosner PJ, Geoghegan KF, Hambor JE., J Clin Invest 97(3), 1996
PMID: 8609233
X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily.
Dhanaraj V, Ye QZ, Johnson LL, Hupe DJ, Ortwine DF, Dunbar JB, Rubin JR, Pavlovsky A, Humblet C, Blundell TL., Structure 4(4), 1996
PMID: 8740360
Dhanaraj V, Ye QZ, Johnson LL, Hupe DJ, Ortwine DF, Dunbar JB, Rubin JR, Pavlovsky A, Humblet C, Blundell TL., Structure 4(4), 1996
PMID: 8740360
Characterization of the 46-kDa intermediates of matrix metalloproteinase 3 (stromelysin 1) obtained by site-directed mutation of phenylalanine 83.
Benbow U, Butticè G, Nagase H, Kurkinen M., J Biol Chem 271(18), 1996
PMID: 8631880
Benbow U, Butticè G, Nagase H, Kurkinen M., J Biol Chem 271(18), 1996
PMID: 8631880
The recombinant catalytic domain of membrane-type matrix metalloproteinase-1 (MT1-MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP-2.
Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett 397(2-3), 1996
PMID: 8955363
Lichte A, Kolkenbrock H, Tschesche H., FEBS Lett 397(2-3), 1996
PMID: 8955363
Activation of precursors for matrix metalloproteinases 1 (interstitial collagenase) and 3 (stromelysin) by rat mast-cell proteinases I and II.
Suzuki K, Lees M, Newlands GF, Nagase H, Woolley DE., Biochem J 305 ( Pt 1)(), 1995
PMID: 7826345
Suzuki K, Lees M, Newlands GF, Nagase H, Woolley DE., Biochem J 305 ( Pt 1)(), 1995
PMID: 7826345
X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design.
Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W., Eur J Biochem 228(3), 1995
PMID: 7737183
Grams F, Reinemer P, Powers JC, Kleine T, Pieper M, Tschesche H, Huber R, Bode W., Eur J Biochem 228(3), 1995
PMID: 7737183
The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.
Stöcker W, Grams F, Baumann U, Reinemer P, Gomis-Rüth FX, McKay DB, Bode W., Protein Sci 4(5), 1995
PMID: 7663339
Stöcker W, Grams F, Baumann U, Reinemer P, Gomis-Rüth FX, McKay DB, Bode W., Protein Sci 4(5), 1995
PMID: 7663339
Structural features of a superfamily of zinc-endopeptidases: the metzincins.
Stöcker W, Bode W., Curr Opin Struct Biol 5(3), 1995
PMID: 7583637
Stöcker W, Bode W., Curr Opin Struct Biol 5(3), 1995
PMID: 7583637
A helping hand for collagenases: the haemopexin-like domain.
Bode W., Structure 3(6), 1995
PMID: 8590012
Bode W., Structure 3(6), 1995
PMID: 8590012
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE., Structure 3(6), 1995
PMID: 8590015
Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE., Structure 3(6), 1995
PMID: 8590015
Rat thimet oligopeptidase: large-scale expression in Escherichia coli and characterization of the recombinant enzyme.
McKie N, Dando PM, Brown MA, Barrett AJ., Biochem J 309 ( Pt 1)(), 1995
PMID: 7619057
McKie N, Dando PM, Brown MA, Barrett AJ., Biochem J 309 ( Pt 1)(), 1995
PMID: 7619057
Proteolytic mechanisms of cartilage breakdown: a target for arthritis therapy?
Buttle DJ, Bramwell H, Hollander AP., Clin Mol Pathol 48(4), 1995
PMID: 16696000
Buttle DJ, Bramwell H, Hollander AP., Clin Mol Pathol 48(4), 1995
PMID: 16696000
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD., Protein Sci 4(10), 1995
PMID: 8535233
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD., Protein Sci 4(10), 1995
PMID: 8535233
Role of the conserved histidine and aspartic acid residues in activity and stabilization of human gelatinase B: an example of matrix metalloproteinases.
Pourmotabbed T, Aelion JA, Tyrrell D, Hasty KA, Bu CH, Mainardi CL., J Protein Chem 14(7), 1995
PMID: 8561849
Pourmotabbed T, Aelion JA, Tyrrell D, Hasty KA, Bu CH, Mainardi CL., J Protein Chem 14(7), 1995
PMID: 8561849
Solution structure of the catalytic domain of human stromelysin complexed with a hydrophobic inhibitor.
Van Doren SR, Kurochkin AV, Hu W, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER., Protein Sci 4(12), 1995
PMID: 8580839
Van Doren SR, Kurochkin AV, Hu W, Ye QZ, Johnson LL, Hupe DJ, Zuiderweg ER., Protein Sci 4(12), 1995
PMID: 8580839
The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H., EMBO J 13(6), 1994
PMID: 8137810
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H., EMBO J 13(6), 1994
PMID: 8137810
Neutrophil procollagenase can be activated by stromelysin-2.
Knäuper V, Murphy G, Tschesche H., Ann N Y Acad Sci 732(), 1994
PMID: 7978810
Knäuper V, Murphy G, Tschesche H., Ann N Y Acad Sci 732(), 1994
PMID: 7978810
Inhibition of matrix metalloproteinases in rheumatoid arthritis and the crystallographic binding mode of a peptide inhibitor.
Tschesche H, Bläser J, Kleine T, Schnierer S, Reinemer P, Bode W, Maasjoshusmann U, Fricke C., Ann N Y Acad Sci 732(), 1994
PMID: 7978819
Tschesche H, Bläser J, Kleine T, Schnierer S, Reinemer P, Bode W, Maasjoshusmann U, Fricke C., Ann N Y Acad Sci 732(), 1994
PMID: 7978819
32 References
Daten bereitgestellt von Europe PubMed Central.
Matrix metalloproteinases and their inhibitors in connective tissue remodeling.
Woessner JF Jr., FASEB J. 5(8), 1991
PMID: 1850705
Woessner JF Jr., FASEB J. 5(8), 1991
PMID: 1850705
Matrisian, Bio Essays 14(), 1992
Matrix metalloproteinases: a review.
Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA., Crit. Rev. Oral Biol. Med. 4(2), 1993
PMID: 8435466
Birkedal-Hansen H, Moore WG, Bodden MK, Windsor LJ, Birkedal-Hansen B, DeCarlo A, Engler JA., Crit. Rev. Oral Biol. Med. 4(2), 1993
PMID: 8435466
The collagen substrate specificity of human neutrophil collagenase.
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG., J. Biol. Chem. 262(21), 1987
PMID: 3038863
Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG., J. Biol. Chem. 262(21), 1987
PMID: 3038863
The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity.
Schnierer S, Kleine T, Gote T, Hillemann A, Knauper V, Tschesche H., Biochem. Biophys. Res. Commun. 191(2), 1993
PMID: 8460992
Schnierer S, Kleine T, Gote T, Hillemann A, Knauper V, Tschesche H., Biochem. Biophys. Res. Commun. 191(2), 1993
PMID: 8460992
Fragmentation of human polymorphonuclear-leucocyte collagenase.
Knauper V, Osthues A, DeClerck YA, Langley KE, Blaser J, Tschesche H., Biochem. J. 291 ( Pt 3)(), 1993
PMID: 8489511
Knauper V, Osthues A, DeClerck YA, Langley KE, Blaser J, Tschesche H., Biochem. J. 291 ( Pt 3)(), 1993
PMID: 8489511
Role of zinc-binding- and hemopexin domain-encoded sequences in the substrate specificity of collagenase and stromelysin-2 as revealed by chimeric proteins.
Sanchez-Lopez R, Alexander CM, Behrendtsen O, Breathnach R, Werb Z., J. Biol. Chem. 268(10), 1993
PMID: 8463259
Sanchez-Lopez R, Alexander CM, Behrendtsen O, Breathnach R, Werb Z., J. Biol. Chem. 268(10), 1993
PMID: 8463259
Biosynthesis and secretion of procollagenase by rabbit synovial fibroblasts. Inhibition of procollagenase secretion by monensin and evidence for glycosylation of procollagenase.
Nagase H, Brinckerhoff CE, Vater CA, Harris ED Jr., Biochem. J. 214(2), 1983
PMID: 6311179
Nagase H, Brinckerhoff CE, Vater CA, Harris ED Jr., Biochem. J. 214(2), 1983
PMID: 6311179
Collagenase is a component of the specific granules of human neutrophil leucocytes.
Murphy G, Reynolds JJ, Bretz U, Baggiolini M., Biochem. J. 162(1), 1977
PMID: 192209
Murphy G, Reynolds JJ, Bretz U, Baggiolini M., Biochem. J. 162(1), 1977
PMID: 192209
Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms.
Knauper V, Kramer S, Reinke H, Tschesche H., Eur. J. Biochem. 189(2), 1990
PMID: 2159879
Knauper V, Kramer S, Reinke H, Tschesche H., Eur. J. Biochem. 189(2), 1990
PMID: 2159879
Secreted forms of human neutrophil collagenase.
Hasty KA, Hibbs MS, Kang AH, Mainardi CL., J. Biol. Chem. 261(12), 1986
PMID: 3007518
Hasty KA, Hibbs MS, Kang AH, Mainardi CL., J. Biol. Chem. 261(12), 1986
PMID: 3007518
The activation of human skin fibroblast procollagenase. Sequence identification of the major conversion products.
Grant GA, Eisen AZ, Marmer BL, Roswit WT, Goldberg GI., J. Biol. Chem. 262(12), 1987
PMID: 3032947
Grant GA, Eisen AZ, Marmer BL, Roswit WT, Goldberg GI., J. Biol. Chem. 262(12), 1987
PMID: 3032947
Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase.
Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE., Biochemistry 29(47), 1990
PMID: 2176876
Mallya SK, Mookhtiar KA, Gao Y, Brew K, Dioszegi M, Birkedal-Hansen H, Van Wart HE., Biochemistry 29(47), 1990
PMID: 2176876
Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin).
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H., Biochemistry 29(44), 1990
PMID: 2176865
Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H., Biochemistry 29(44), 1990
PMID: 2176865
Mercurial activation of human polymorphonuclear leucocyte procollagenase.
Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H., Eur. J. Biochem. 202(3), 1991
PMID: 1662606
Blaser J, Knauper V, Osthues A, Reinke H, Tschesche H., Eur. J. Biochem. 202(3), 1991
PMID: 1662606
Direct activation of human neutrophil procollagenase by recombinant stromelysin.
Knauper V, Wilhelm SM, Seperack PK, DeClerck YA, Langley KE, Osthues A, Tschesche H., Biochem. J. 295 ( Pt 2)(), 1993
PMID: 8240261
Knauper V, Wilhelm SM, Seperack PK, DeClerck YA, Langley KE, Osthues A, Tschesche H., Biochem. J. 295 ( Pt 2)(), 1993
PMID: 8240261
Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes.
Murphy G, Cockett MI, Stephens PE, Smith BJ, Docherty AJ., Biochem. J. 248(1), 1987
PMID: 2829822
Murphy G, Cockett MI, Stephens PE, Smith BJ, Docherty AJ., Biochem. J. 248(1), 1987
PMID: 2829822
Tissue cooperation in a proteolytic cascade activating human interstitial collagenase.
HE CS, Wilhelm SM, Pentland AP, Marmer BL, Grant GA, Eisen AZ, Goldberg GI., Proc. Natl. Acad. Sci. U.S.A. 86(8), 1989
PMID: 2468156
HE CS, Wilhelm SM, Pentland AP, Marmer BL, Grant GA, Eisen AZ, Goldberg GI., Proc. Natl. Acad. Sci. U.S.A. 86(8), 1989
PMID: 2468156
Bode, EMBO J. (), 1994
Purification of human collagenases with a hydroxamic acid affinity column.
Moore WM, Spilburg CA., Biochemistry 25(18), 1986
PMID: 3021211
Moore WM, Spilburg CA., Biochemistry 25(18), 1986
PMID: 3021211
AUTHOR UNKNOWN, 0
AUTHOR UNKNOWN, 0
Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases.
Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL., J. Biol. Chem. 265(20), 1990
PMID: 2164002
Hasty KA, Pourmotabbed TF, Goldberg GI, Thompson JP, Spinella DG, Stevens RM, Mainardi CL., J. Biol. Chem. 265(20), 1990
PMID: 2164002
Jones, J. Appl. Crystallogr. 15(), 1978
Brünger, Acta Cryst. Sect. A 45(), 1989
Engh, Acta Cryst. Sect. A 47(), 1991
First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases.
Gomis-Ruth FX, Kress LF, Bode W., EMBO J. 12(11), 1993
PMID: 8223430
Gomis-Ruth FX, Kress LF, Bode W., EMBO J. 12(11), 1993
PMID: 8223430
Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'.
Bode W, Gomis-Ruth FX, Stockler W., FEBS Lett. 331(1-2), 1993
PMID: 8405391
Bode W, Gomis-Ruth FX, Stockler W., FEBS Lett. 331(1-2), 1993
PMID: 8405391
Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases.
Bode W, Gomis-Ruth FX, Huber R, Zwilling R, Stocker W., Nature 358(6382), 1992
PMID: 1319561
Bode W, Gomis-Ruth FX, Huber R, Zwilling R, Stocker W., Nature 358(6382), 1992
PMID: 1319561
Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin.
Gomis-Ruth FX, Stocker W, Huber R, Zwilling R, Bode W., J. Mol. Biol. 229(4), 1993
PMID: 8445658
Gomis-Ruth FX, Stocker W, Huber R, Zwilling R, Bode W., J. Mol. Biol. 229(4), 1993
PMID: 8445658
Priestle, J. Appl. Crystallogr. 21(), 1988
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.
Kabsch W, Sander C., Biopolymers 22(12), 1983
PMID: 6667333
Kabsch W, Sander C., Biopolymers 22(12), 1983
PMID: 6667333
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