Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure

Lang R, Kocourek A, Braun M, Tschesche H, Huber R, Bode W, Maskos K (2001)
JOURNAL OF MOLECULAR BIOLOGY 312(4): 731-742.

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DOI
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
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Einrichtung
Fakultät für Chemie > Biochemie I
Abstract / Bemerkung
The macrophage elastase enzyme (MMP-12) expressed mainly in alveolar macrophages has been identified in the mouse lung as the main destructive agent associated with cigarette smoking, which gives rise to emphysema, both directly via elastin degradation and indirectly by disturbing the proteinase/antiproteinase balance via inactivation of the alpha1-proteinase inhibitor (alpha1-PI), the antagonist of the leukocyte elastase. The catalytic domain of human recombinant MMP-12 has been crystallized in complex with the broad-specificity inhibitor batimastat (BB-94). The crystal structure analysis of this complex, determined using X-ray data to 1.1 Angstrom and refined to an R-value of 0.165, reveals an overall fold similar to that of other MMPs. However, the S-shaped double loop connecting strands III and IV is fixed closer to the beta -sheet and projects its His172 side-chain further into the rather hydrophobic active-site cleft, defining the S3 and the S1-pockets and separating them from each other to a larger extent than is observed in other MMPs. The S2-site is planar, while the characteristic S1'-subsite is a continuous tube rather than a pocket, in which the MMP-12-specific Thr215 replaces a Val residue otherwise highly conserved in almost all other MMPs. This alteration might allow MMP-12 to accept P1' Arg residues, making it unique among MMPs. The active-site cleft of MMP-12 is well equipped to bind and efficiently cleave the AlaMetPhe-LeuGluAla sequence in the reactive-site loop of al-PI, as occurs experimentally. Similarities in contouring and particularly a common surface hydrophobicity both inside and distant from the active-site cleft explain why MMP-12 shares many substrates with matrilysin (MMP-7). The MMP-12 structure is an excellent template for the structure-based design of specific inhibitors for emphysema therapy and for the construction of mutants to clarify the role of this MMP. (C) 2001 Academic Press.
Stichworte
emphysema; matrix metalloproteinase; alpha; 1-proteinase inhibitor; crystal structure; elastase
Erscheinungsjahr
2001
Zeitschriftentitel
JOURNAL OF MOLECULAR BIOLOGY
Band
312
Zeitschriftennummer
4
Seite
731-742
ISSN
0022-2836
PUB-ID

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Lang R, Kocourek A, Braun M, et al. Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure. JOURNAL OF MOLECULAR BIOLOGY. 2001;312(4):731-742.
Lang, R., Kocourek, A., Braun, M., Tschesche, H., Huber, R., Bode, W., & Maskos, K. (2001). Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure. JOURNAL OF MOLECULAR BIOLOGY, 312(4), 731-742. doi:10.1006/jmbi.2001.4954
Lang, R., Kocourek, A., Braun, M., Tschesche, H., Huber, R., Bode, W., and Maskos, K. (2001). Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure. JOURNAL OF MOLECULAR BIOLOGY 312, 731-742.
Lang, R., et al., 2001. Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure. JOURNAL OF MOLECULAR BIOLOGY, 312(4), p 731-742.
R. Lang, et al., “Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure”, JOURNAL OF MOLECULAR BIOLOGY, vol. 312, 2001, pp. 731-742.
Lang, R., Kocourek, A., Braun, M., Tschesche, H., Huber, R., Bode, W., Maskos, K.: Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure. JOURNAL OF MOLECULAR BIOLOGY. 312, 731-742 (2001).
Lang, R, Kocourek, A, Braun, M, Tschesche, Harald, Huber, R, Bode, W, and Maskos, K. “Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 angstrom crystal structure”. JOURNAL OF MOLECULAR BIOLOGY 312.4 (2001): 731-742.

48 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Synthesis and binding monitoring of a new nanomolar PAMAM-based matrix metalloproteinases inhibitor (MMPIs).
Cerofolini L, Baldoneschi V, Dragoni E, Storai A, Mamusa M, Berti D, Fragai M, Richichi B, Nativi C., Bioorg Med Chem 25(2), 2017
PMID: 27914947
Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.
Fulcher YG, Prior SH, Masuko S, Li L, Pu D, Zhang F, Linhardt RJ, Van Doren SR., Structure 25(7), 2017
PMID: 28648610
Fluorescent Analogue of Batimastat Enables Imaging of α-Secretase in Living Cells.
Leriche G, Chen AC, Kim S, Selkoe DJ, Yang J., ACS Chem Neurosci 7(1), 2016
PMID: 26559179
Matrix metalloproteinases as input and output signals for post-myocardial infarction remodeling.
Lindsey ML, Iyer RP, Jung M, DeLeon-Pennell KY, Ma Y., J Mol Cell Cardiol 91(), 2016
PMID: 26721597
Pseudo-Contact NMR Shifts over the Paramagnetic Metalloprotein CoMMP-12 from First Principles.
Benda L, Mareš J, Ravera E, Parigi G, Luchinat C, Kaupp M, Vaara J., Angew Chem Int Ed Engl 55(47), 2016
PMID: 27781358
Up-regulation of matrix metallopeptidase 12 in motor neurons undergoing synaptic stripping.
Sajjan S, Holsinger RM, Fok S, Ebrahimkhani S, Rollo JL, Banati RB, Graeber MB., Neuroscience 274(), 2014
PMID: 24907602
Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.
Koppisetti RK, Fulcher YG, Jurkevich A, Prior SH, Xu J, Lenoir M, Overduin M, Van Doren SR., Nat Commun 5(), 2014
PMID: 25412686
Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease.
Zhang L, Conway JF, Thibodeau PH., J Biol Chem 287(6), 2012
PMID: 22170064
Structural signatures of enzyme binding pockets from order-independent surface alignment: a study of metalloendopeptidase and NAD binding proteins.
Dundas J, Adamian L, Liang J., J Mol Biol 406(5), 2011
PMID: 21145898
Global gene expression profile progression in Gaucher disease mouse models.
Xu YH, Jia L, Quinn B, Zamzow M, Stringer K, Aronow B, Sun Y, Zhang W, Setchell KD, Grabowski GA., BMC Genomics 12(), 2011
PMID: 21223590
Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.
Fulcher YG, Van Doren SR., Biochemistry 50(44), 2011
PMID: 21967233
Degradation of tropoelastin by matrix metalloproteinases--cleavage site specificities and release of matrikines.
Heinz A, Jung MC, Duca L, Sippl W, Taddese S, Ihling C, Rusciani A, Jahreis G, Weiss AS, Neubert RH, Schmelzer CE., FEBS J 277(8), 2010
PMID: 20345904
Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.
Liang X, Arunima A, Zhao Y, Bhaskaran R, Shende A, Byrne TS, Fleeks J, Palmier MO, Van Doren SR., Biophys J 99(1), 2010
PMID: 20655856
Inhibitory effect of quercetin on matrix metalloproteinase 9 activity molecular mechanism and structure-activity relationship of the flavonoid-enzyme interaction.
Saragusti AC, Ortega MG, Cabrera JL, Estrin DA, Marti MA, Chiabrando GA., Eur J Pharmacol 644(1-3), 2010
PMID: 20619256
NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.
Palmier MO, Fulcher YG, Bhaskaran R, Duong VQ, Fields GB, Van Doren SR., J Biol Chem 285(40), 2010
PMID: 20663866
A mathematical model of protease-antiprotease homeostasis failure in chronic obstructive pulmonary disease (COPD).
Cox LA., Risk Anal 29(4), 2009
PMID: 19000077
In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24.
Taddese S, Weiss AS, Jahreis G, Neubert RH, Schmelzer CE., Matrix Biol 28(2), 2009
PMID: 19144321
Amidation of bioactive peptides: the structure of the lyase domain of the amidating enzyme.
Chufán EE, De M, Eipper BA, Mains RE, Amzel LM., Structure 17(7), 2009
PMID: 19604476
In silico study of MMP inhibition.
Rouffet M, Denhez C, Bourguet E, Bohr F, Guillaume D., Org Biomol Chem 7(18), 2009
PMID: 19707688
Characterisation of the MMP-12-elastin adduct.
Bertini I, Fragai M, Luchinat C, Melikian M, Venturi C., Chemistry 15(32), 2009
PMID: 19609998
Mapping of macrophage elastase cleavage sites in insoluble human skin elastin.
Taddese S, Weiss AS, Neubert RH, Schmelzer CE., Matrix Biol 27(5), 2008
PMID: 18334288
A peptide hydroxamate library for enrichment of metalloproteinases: towards an affinity-based metalloproteinase profiling protocol.
Geurink P, Klein T, Leeuwenburgh M, van der Marel G, Kauffman H, Bischoff R, Overkleeft H., Org Biomol Chem 6(7), 2008
PMID: 18362965
Evolution of binding sites for zinc and calcium ions playing structural roles.
Torrance JW, Macarthur MW, Thornton JM., Proteins 71(2), 2008
PMID: 18004751
MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
Bhaskaran R, Palmier MO, Lauer-Fields JL, Fields GB, Van Doren SR., J Biol Chem 283(31), 2008
PMID: 18539597
Expression and regulation of matrix metalloproteinase-12 in experimental autoimmune encephalomyelitis and by bone marrow derived macrophages in vitro.
Dasilva AG, Yong VW., J Neuroimmunol 199(1-2), 2008
PMID: 18547653
Molecular determinants of matrix metalloproteinase-12 covalent modification by a photoaffinity probe: insights into activity-based probe development and conformational variability of matrix metalloproteinases.
Dabert-Gay AS, Czarny B, Devel L, Beau F, Lajeunesse E, Bregant S, Thai R, Yiotakis A, Dive V., J Biol Chem 283(45), 2008
PMID: 18775985
Substrate specificity of a metalloprotease of the pappalysin family revealed by an inhibitor and a product complex.
García-Castellanos R, Tallant C, Marrero A, Solà M, Baumann U, Gomis-Rüth FX., Arch Biochem Biophys 457(1), 2007
PMID: 17097044
The design of inhibitors for medicinally relevant metalloproteins.
Jacobsen FE, Lewis JA, Cohen SM., ChemMedChem 2(2), 2007
PMID: 17163561
Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion.
Lee S, Park HI, Sang QX., Biochem J 403(1), 2007
PMID: 17176253
Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment.
Bhaskaran R, Palmier MO, Bagegni NA, Liang X, Van Doren SR., J Mol Biol 374(5), 2007
PMID: 17997411
Design and characterization of a metalloproteinase inhibitor-tethered resin for the detection of active MMPs in biological samples.
Hesek D, Toth M, Meroueh SO, Brown S, Zhao H, Sakr W, Fridman R, Mobashery S., Chem Biol 13(4), 2006
PMID: 16632250
Synthesis of bicyclic molecular scaffolds (BTAa): an investigation towards new selective MMP-12 inhibitors.
Mannino C, Nievo M, Machetti F, Papakyriakou A, Calderone V, Fragai M, Guarna A., Bioorg Med Chem 14(22), 2006
PMID: 16899369
Characterization of Ca2+ interactions with matrix metallopeptidase-12: implications for matrix metallopeptidase regulation.
Gossas T, Danielson UH., Biochem J 398(3), 2006
PMID: 16737445
Altered postnatal lung development in C3H/HeJ mice.
Sampath V, Davis K, Senft AP, Richardson TR, Kitzmiller JA, Berclaz PY, Korfhagen TR., Pediatr Res 60(6), 2006
PMID: 17065580
Structural basis for the highly selective inhibition of MMP-13.
Engel CK, Pirard B, Schimanski S, Kirsch R, Habermann J, Klingler O, Schlotte V, Weithmann KU, Wendt KU., Chem Biol 12(2), 2005
PMID: 15734645
Crystal structures of MMPs in complex with physiological and pharmacological inhibitors.
Maskos K., Biochimie 87(3-4), 2005
PMID: 15781312
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
Conformational variability of matrix metalloproteinases: beyond a single 3D structure.
Bertini I, Calderone V, Cosenza M, Fragai M, Lee YM, Luchinat C, Mangani S, Terni B, Turano P., Proc Natl Acad Sci U S A 102(15), 2005
PMID: 15809432
Structure-based design and synthesis of novel non-zinc chelating MMP-12 inhibitors.
Dublanchet AC, Ducrot P, Andrianjara C, O'Gara M, Morales R, Compère D, Denis A, Blais S, Cluzeau P, Courté K, Hamon J, Moreau F, Prunet ML, Tertre A., Bioorg Med Chem Lett 15(16), 2005
PMID: 16002291
Similarity of binding sites of human matrix metalloproteinases.
Lukacova V, Zhang Y, Mackov M, Baricic P, Raha S, Calvo JA, Balaz S., J Biol Chem 279(14), 2004
PMID: 14732707
Crystal structure of the catalytic domain of human matrix metalloproteinase 10.
Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B., J Mol Biol 336(3), 2004
PMID: 15095982
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.
Kruse MN, Becker C, Lottaz D, Köhler D, Yiallouros I, Krell HW, Sterchi EE, Stöcker W., Biochem J 378(pt 2), 2004
PMID: 14594449
Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12.
Morales R, Perrier S, Florent JM, Beltra J, Dufour S, De Mendez I, Manceau P, Tertre A, Moreau F, Compere D, Dublanchet AC, O'Gara M., J Mol Biol 341(4), 2004
PMID: 15289103
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
Activity-based enrichment of matrix metalloproteinases using reversible inhibitors as affinity ligands.
Freije JR, Bischoff R., J Chromatogr A 1009(1-2), 2003
PMID: 13677656
The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling.
Park HI, Jin Y, Hurst DR, Monroe CA, Lee S, Schwartz MA, Sang QX., J Biol Chem 278(51), 2003
PMID: 14532275
Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases.
Maskos K, Bode W., Mol Biotechnol 25(3), 2003
PMID: 14668538
Modified AutoDock for accurate docking of protein kinase inhibitors.
Buzko OV, Bishop AC, Shokat KM., J Comput Aided Mol Des 16(2), 2002
PMID: 12188021

58 References

Daten bereitgestellt von Europe PubMed Central.


Barrett, 1998
Matrix metalloproteinases.
Nagase H, Woessner JF Jr., J. Biol. Chem. 274(31), 1999
PMID: 10419448
Insights into MMP-TIMP interactions
Bode, Ann. NY Acad. Sci. 878(), 1999
Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII.
Hiller O, Lichte A, Oberpichler A, Kocourek A, Tschesche H., J. Biol. Chem. 275(42), 2000
PMID: 10930399
The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo.
Liu Z, Zhou X, Shapiro SD, Shipley JM, Twining SS, Diaz LA, Senior RM, Werb Z., Cell 102(5), 2000
PMID: 11007483
Structural properties of matrix metalloproteinases.
Bode W, Fernandez-Catalan C, Tschesche H, Grams F, Nagase H, Maskos K., Cell. Mol. Life Sci. 55(4), 1999
PMID: 10357232
Structure and promoter characterization of the human membrane-type-1 matrix metalloproteinase (mt1-mmp) gene
Lohi, Gene 242(), 1998
MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors.
Marchenko GN, Strongin AY., Gene 265(1-2), 2001
PMID: 11255011
Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms.
Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW., J. Clin. Invest. 102(11), 1998
PMID: 9835614
Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice
Shipley, Proc. Nat. Acad. Sci. USA 93(), 1996
Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase.
Gronski TJ Jr, Martin RL, Kobayashi DK, Walsh BC, Holman MC, Huber M, Van Wart HE, Shapiro SD., J. Biol. Chem. 272(18), 1997
PMID: 9115292
Animal models for chronic obstructive pulmonary disease: age of klotho and marlboro mice.
Shapiro SD., Am. J. Respir. Cell Mol. Biol. 22(1), 2000
PMID: 10615058
Human collagenase (matrix metalloproteinase-1) expression in the lungs of patients with emphysema.
Imai K, Dalal SS, Chen ES, Downey R, Schulman LL, Ginsburg M, D'Armiento J., Am. J. Respir. Crit. Care Med. 163(3 Pt 1), 2001
PMID: 11254539
Diverse roles of macrophage matrix metalloproteinases in tissue destruction and tumor growth.
Shapiro SD., Thromb. Haemost. 82(2), 1999
PMID: 10605792
Alpha 1-proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase.
Banda MJ, Rice AG, Griffin GL, Senior RM., J. Biol. Chem. 263(9), 1988
PMID: 3257965
Human plasma proteinase inhibitors.
Travis J, Salvesen GS., Annu. Rev. Biochem. 52(), 1983
PMID: 6193754
Matrix metalloproteinases generate angiostatin: effects on neovascularization.
Cornelius LA, Nehring LC, Harding E, Bolanowski M, Welgus HG, Kobayashi DK, Pierce RA, Shapiro SD., J. Immunol. 161(12), 1998
PMID: 9862716
Macrophage metalloelastase degrades matrix and myelin proteins and processes a tumour necrosis factor-alpha fusion protein.
Chandler S, Cossins J, Lury J, Wells G., Biochem. Biophys. Res. Commun. 228(2), 1996
PMID: 8920930
Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice.
Hautamaki RD, Kobayashi DK, Senior RM, Shapiro SD., Science 277(5334), 1997
PMID: 9302297
Structural studies on MMPs and TIMPs.
Bode W, Maskos K., Methods Mol. Biol. 151(), 2001
PMID: 11217319
Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages.
Shapiro SD, Kobayashi DK, Ley TJ., J. Biol. Chem. 268(32), 1993
PMID: 8226919
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., FEBS Lett. 338(2), 1994
PMID: 8307185
Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.
Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K., Science 284(5420), 1999
PMID: 10356396
Matrilysin-inhibitor complexes: common themes among metalloproteases.
Browner MF, Smith WW, Castelhano AL., Biochemistry 34(20), 1995
PMID: 7756291
3D search and research using the Cambridge Structural Database
Allen, Chemical Des. Autom. News 8(), 1993
Structure determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor.
Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W., Biochemistry 34(43), 1995
PMID: 7577999
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

Glusker, 1994
Characterization of zinc-binding sites in human stromelysin-1: stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme.
Salowe SP, Marcy AI, Cuca GC, Smith CK, Kopka IE, Hagmann WK, Hermes JD., Biochemistry 31(19), 1992
PMID: 1581308
The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: a possible role for the C-terminal domain.
Willenbrock F, Murphy G, Phillips IR, Brocklehurst K., FEBS Lett. 358(2), 1995
PMID: 7828734
Structural characterization of the catalytic active site in the latent and active natural gelatinase B from human neutrophils.
Kleifeld O, Van den Steen PE, Frenkel A, Cheng F, Jiang HL, Opdenakker G, Sagi I., J. Biol. Chem. 275(44), 2000
PMID: 10938090
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
Calcium-binding sites in proteins
McPhalen, Advan. Protein Chem. 42(), 1991
Elastin degradation by matrix metalloproteinases. Cleavage site specificity and mechanisms of elastolysis.
Mecham RP, Broekelmann TJ, Fliszar CJ, Shapiro SD, Welgus HG, Senior RM., J. Biol. Chem. 272(29), 1997
PMID: 9218437
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Gomis-Ruth FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K, Bourenkov GP, Bartunik H, Bode W., Nature 389(6646), 1997
PMID: 9288970
Matrilysin is much more efficient than other matrix metalloproteinases in the proteolytic inactivation of alpha 1-antitrypsin.
Sires UI, Murphy G, Baragi VM, Fliszar CJ, Welgus HG, Senior RM., Biochem. Biophys. Res. Commun. 204(2), 1994
PMID: 7980522
Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma.
Dong Z, Kumar R, Yang X, Fidler IJ., Cell 88(6), 1997
PMID: 9118223
Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9).
Patterson BC, Sang QA., J. Biol. Chem. 272(46), 1997
PMID: 9360944
Accumulation of matrilysin (MMP-7) and macrophage metalloelastase (MMP-12) in actinic damage.
Saarialho-Kere U, Kerkela E, Jeskanen L, Hasan T, Pierce R, Starcher B, Raudasoja R, Ranki A, Oikarinen A, Vaalamo M., J. Invest. Dermatol. 113(4), 1999
PMID: 10504457
Interferon gamma induction of pulmonary emphysema in the adult murine lung.
Wang Z, Zheng T, Zhu Z, Homer RJ, Riese RJ, Chapman HA Jr, Shapiro SD, Elias JA., J. Exp. Med. 192(11), 2000
PMID: 11104801
A general method of in vitro preparation and specific mutagenesis of DNA fragments
Higuchi, Nucl. Acids Res. 16(), 1988
Purification of human collagenases with a hydroxamic acid affinity column.
Moore WM, Spilburg CA., Biochemistry 25(18), 1986
PMID: 3021211
TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3.
Amour A, Slocombe PM, Webster A, Butler M, Knight CG, Smith BJ, Stephens PE, Shelley C, Hutton M, Knauper V, Docherty AJ, Murphy G., FEBS Lett. 435(1), 1998
PMID: 9755855
Solvent content of protein crystals.
Matthews BW., J. Mol. Biol. 33(2), 1968
PMID: 5700707
Processing of X-ray diffraction data collected in oscillations mode
Otwinowski, Methods Enzymol. 276(), 1997
AMoRe
Navaza, Acta Crystallog. sect. A 50(), 1994

Brünger, 1992
Accurate bond and angle parameters for X-ray protein structure refinement
Engh, Acta Crystallog. sect. D 4(), 1991
Crystallography and NMR systems (CNS)
Brünger, Acta Crystallog. sect. D 54(), 1998
Improved methods for building protein models in electron density maps and the location of errors in these models
Jones, Acta Crystallog. sect. A 47(), 1991
SHELXL: high-resolution refinement.
Sheldrick GM, Schneider TR., Meth. Enzymol. 277(), 1997
PMID: 18488315
The CCP4 suite,programs for protein crystallography
AUTHOR UNKNOWN, Acta Crystallog. sect. D 50(), 1994

McRee, 1993
PROCHECK: a program to check the stereochemical quality of protein structures.
Laskowski RA, MacArthur MW, Moss DS, Thornton JM., J Appl Crystallogr 26(2), 1993
PMID: c6802
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities.
Esnouf RM., J. Mol. Graph. Model. 15(2), 1997
PMID: 9385560
Raster3D version 2.0. A program for photorealistic molecular graphics
Merritt, Acta Crystallog. sect. D 50(), 1994
ALSCRIPT: a tool to format multiple sequence alignments.
Barton GJ., Protein Eng. 6(1), 1993
PMID: 8433969
Swiss-PDBViewer
Guex, PDB Quart. Newsletter 77(), 1996

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