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 (1995)
BIOCHEMISTRY 34(43): 14012-14020.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ; ;
Abstract / Bemerkung
Matrix metalloproteinases are a family of zinc endopeptidases involved in tissue remodeling. They have been implicated in various disease processes including metastasis, joint destruction, and neurodegeneration, Human neutrophil collagenase (HNC, MMP-8) represents one of the three ''interstitial'' collagenases that cleave triple-helical collagens types I, II, and III. Its 163-residue catalytic domain (Met80 to Gly242) has been expressed in Escherichia coli and crystallized as a noncovalent complex with the hydroxamate inhibitor batimastat. The crystal structure, refined to 2.1 Angstrom, demonstrates that batimastat binds to the S1-S2' sites and coordinates to the catalytic zinc in a bidentate manner via the hydroxyl and carbonyl oxygens of the hydroxamate group. The batimastat-collagenase complex is described in detail, and the activities of batimastat analogues are discussed in the light of the protein-inhibitor interactions revealed by the crystallography studies,
Erscheinungsjahr
Zeitschriftentitel
BIOCHEMISTRY
Band
34
Ausgabe
43
Seite(n)
14012-14020
ISSN
eISSN
PUB-ID

Zitieren

GRAMS F, CRIMMIN M, HINNES L, et al. STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR. BIOCHEMISTRY. 1995;34(43):14012-14020.
GRAMS, F., CRIMMIN, M., HINNES, L., HUXLEY, P., PIEPER, M., Tschesche, H., & BODE, W. (1995). STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR. BIOCHEMISTRY, 34(43), 14012-14020. doi:10.1021/bi00043a007
GRAMS, F., CRIMMIN, M., HINNES, L., HUXLEY, P., PIEPER, M., Tschesche, H., and BODE, W. (1995). STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR. BIOCHEMISTRY 34, 14012-14020.
GRAMS, F., et al., 1995. STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR. BIOCHEMISTRY, 34(43), p 14012-14020.
F. GRAMS, et al., “STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR”, BIOCHEMISTRY, vol. 34, 1995, pp. 14012-14020.
GRAMS, F., CRIMMIN, M., HINNES, L., HUXLEY, P., PIEPER, M., Tschesche, H., BODE, W.: STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR. BIOCHEMISTRY. 34, 14012-14020 (1995).
GRAMS, F, CRIMMIN, M, HINNES, L, HUXLEY, P, PIEPER, M, Tschesche, Harald, and BODE, W. “STRUCTURE DETERMINATION AND ANALYSIS OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED WITH A HYDROXAMATE INHIBITOR”. BIOCHEMISTRY 34.43 (1995): 14012-14020.

59 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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
Therapeutic potential of matrix metalloproteinases in Duchenne muscular dystrophy.
Ogura Y, Tajrishi MM, Sato S, Hindi SM, Kumar A., Front Cell Dev Biol 2(), 2014
PMID: 25364719
Shedding of discoidin domain receptor 1 by membrane-type matrix metalloproteinases.
Fu HL, Sohail A, Valiathan RR, Wasinski BD, Kumarasiri M, Mahasenan KV, Bernardo MM, Tokmina-Roszyk D, Fields GB, Mobashery S, Fridman R., J Biol Chem 288(17), 2013
PMID: 23519472
Novel hydroxamic acid-related phosphinates: inhibition of neutral aminopeptidase N (APN).
Drag M, Grzywa R, Oleksyszyn J., Bioorg Med Chem Lett 17(6), 2007
PMID: 17270439
Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I.
Temperini C, Innocenti A, Guerri A, Scozzafava A, Rusconi S, Supuran CT., Bioorg Med Chem Lett 17(8), 2007
PMID: 17314045
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
N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8.
Campestre C, Agamennone M, Tortorella P, Preziuso S, Biasone A, Gavuzzo E, Pochetti G, Mazza F, Hiller O, Tschesche H, Consalvi V, Gallina C., Bioorg Med Chem Lett 16(1), 2006
PMID: 16242329
Amber force field implementation, molecular modelling study, synthesis and MMP-1/MMP-2 inhibition profile of (R)- and (S)-N-hydroxy-2-(N-isopropoxybiphenyl-4-ylsulfonamido)-3-methylbutanamides.
Tuccinardi T, Martinelli A, Nuti E, Carelli P, Balzano F, Uccello-Barretta G, Murphy G, Rossello A., Bioorg Med Chem 14(12), 2006
PMID: 16483784
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
N-hydroxyurea--a versatile zinc binding function in the design of metalloenzyme inhibitors.
Temperini C, Innocenti A, Scozzafava A, Supuran CT., Bioorg Med Chem Lett 16(16), 2006
PMID: 16759856
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
A combination of docking, QM/MM methods, and MD simulation for binding affinity estimation of metalloprotein ligands.
Khandelwal A, Lukacova V, Comez D, Kroll DM, Raha S, Balaz S., J Med Chem 48(17), 2005
PMID: 16107143
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
A practical approach to docking of zinc metalloproteinase inhibitors.
Hu X, Balaz S, Shelver WH., J Mol Graph Model 22(4), 2004
PMID: 15177081
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
Hydroxyurea is a carbonic anhydrase inhibitor.
Scozzafava A, Supuran CT., Bioorg Med Chem 11(10), 2003
PMID: 12713833
Structural aspects of the metzincin clan of metalloendopeptidases.
Gomis-Rüth FX., Mol Biotechnol 24(2), 2003
PMID: 12746556
Design and synthesis of dual inhibitors for matrix metalloproteinase and cathepsin.
Yamamoto M, Ikeda S, Kondo H, Inoue S., Bioorg Med Chem Lett 12(3), 2002
PMID: 11814800
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
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
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
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
A comparative docking study and the design of potentially selective MMP inhibitors.
Hanessian S, Moitessier N, Therrien E., J Comput Aided Mol Des 15(10), 2001
PMID: 11918074
Collagenolytic and gelatinolytic matrix metalloproteinases and their inhibitors in basal cell carcinoma of skin: comparison with normal skin.
Varani J, Hattori Y, Chi Y, Schmidt T, Perone P, Zeigler ME, Fader DJ, Johnson TM., Br J Cancer 82(3), 2000
PMID: 10682680
Ongoing trials with matrix metalloproteinase inhibitors.
Brown PD., Expert Opin Investig Drugs 9(9), 2000
PMID: 11060801
Picking the S1, S1' and S2' pockets of matrix metalloproteinases. A niche for potent acyclic sulfonamide inhibitors.
Hanessian S, Bouzbouz S, Boudon A, Tucker GC, Peyroulan D., Bioorg Med Chem Lett 9(12), 1999
PMID: 10397503
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
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors.
Finnin MS, Donigian JR, Cohen A, Richon VM, Rifkind RA, Marks PA, Breslow R, Pavletich NP., Nature 401(6749), 1999
PMID: 10490031
Crystal structure of the stromelysin catalytic domain at 2.0 A resolution: inhibitor-induced conformational changes.
Chen L, Rydel TJ, Gu F, Dunaway CM, Pikul S, Dunham KM, Barnett BL., J Mol Biol 293(3), 1999
PMID: 10543949
A fluorescence resonance energy transfer method for measuring the binding of inhibitors to stromelysin.
Epps DE, Mitchell MA, Petzold GL, VanDrie JH, Poorman RA., Anal Biochem 275(2), 1999
PMID: 10552897
Matrix metalloproteases: variations on a theme.
Borkakoti N., Prog Biophys Mol Biol 70(1), 1998
PMID: 9785958
Selective inhibition of low affinity IgE receptor (CD23) processing.
Bailey S, Bolognese B, Buckle DR, Faller A, Jackson S, Louis-Flamberg P, McCord M, Mayer RJ, Marshall LA, Smith DG., Bioorg Med Chem Lett 8(1), 1998
PMID: 9871623
Matrix metalloproteinase inhibitors.
Brown PD., Breast Cancer Res Treat 52(1-3), 1998
PMID: 10066077
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
The design, synthesis, and structure-activity relationships of a series of macrocyclic MMP inhibitors.
Steinman DH, Curtin ML, Garland RB, Davidsen SK, Heyman HR, Holms JH, Albert DH, Magoc TJ, Nagy IB, Marcotte PA, Li J, Morgan DW, Hutchins C, Summers JB., Bioorg Med Chem Lett 8(16), 1998
PMID: 9873491
Structural characterizations of nonpeptidic thiadiazole inhibitors of matrix metalloproteinases reveal the basis for stromelysin selectivity.
Finzel BC, Baldwin ET, Bryant GL, Hess GF, Wilks JW, Trepod CM, Mott JE, Marshall VP, Petzold GL, Poorman RA, O'Sullivan TJ, Schostarez HJ, Mitchell MA., Protein Sci 7(10), 1998
PMID: 9792098
The constituent tryptophans and bisANS as fluorescent probes of the active site and of a secondary binding site of stromelysin-1 (MMP-3).
Epps DE, Poorman RA, Petzold GL, Stuchly CW, Laborde AL, Van Drie JH., J Protein Chem 17(7), 1998
PMID: 9853686
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
2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode.
Cirilli M, Gallina C, Gavuzzo E, Giordano C, Gomis-Rüth FX, Gorini B, Kress LF, Mazza F, Paradisi MP, Pochetti G, Politi V., FEBS Lett 418(3), 1997
PMID: 9428736
Non-peptidic cysteine derivatives as inhibitors of matrix metalloproteinases.
Müller JC, von Roedern EG, Grams F, Nagase H, Moroder L., Biol Chem 378(12), 1997
PMID: 9461346
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF., Proc Natl Acad Sci U S A 93(7), 1996
PMID: 8610113

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 7577999
PubMed | Europe PMC

Suchen in

Google Scholar