THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY

BODE W, REINEMER P, HUBER R, KLEINE T, SCHNIERER S, Tschesche H (1994)
EMBO JOURNAL 13(6): 1263-1269.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Matrix metalloproteinases are a family of zinc endopeptidases involved in tissue remodelling. They have been implicated in various disease processes including tumour invasion and joint destruction. These enzymes consist of several domains, which are responsible for latency, catalysis and substrate recognition. Human neutrophil collagenase (PMNL-CL, MMP-8) represents one of the two '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 non-covalent complex with the inhibitor Pro-Leu-Gly-hydroxylamine. The 2.0 angstrom crystal structure reveals a spherical molecule with a shallow active-site cleft separating a smaller C-terminal subdomain from a bigger N-terminal domain, composed of a rive-stranded beta-sheet, two alpha-helices, and bridging loops. The inhibitor mimics the unprimed (P1-P3) residues of a substrate; primed (P1'-P3') peptide substrate residues should bind in an extended conformation, with the bulky P1' side-chain fitting into the deep hydrophobic S1' subsite. Modelling experiments with collagen show that the scissile strand of triple-helical collagen must be freed to fit the subsites. The catalytic zinc ion is situated at the bottom of the active-site cleft and is penta-coordinated by three histidines and by both hydroxamic acid oxygens of the inhibitor. In addition to the catalytic zinc, the catalytic domain harbours a second, non-exchangeable zinc ion and two calcium ions, which are packed against the top of the beta-sheet and presumably function to stabilize the catalytic domain. The polypeptide folding and in particular the zinc environment of the collagenase catalytic domain bear a close resemblance to the astacins and the snake venom metalloproteinases.
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Zeitschriftentitel
EMBO JOURNAL
Band
13
Zeitschriftennummer
6
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1263-1269
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BODE W, REINEMER P, HUBER R, KLEINE T, SCHNIERER S, Tschesche H. THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY. EMBO JOURNAL. 1994;13(6):1263-1269.
BODE, W., REINEMER, P., HUBER, R., KLEINE, T., SCHNIERER, S., & Tschesche, H. (1994). THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY. EMBO JOURNAL, 13(6), 1263-1269.
BODE, W., REINEMER, P., HUBER, R., KLEINE, T., SCHNIERER, S., and Tschesche, H. (1994). THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY. EMBO JOURNAL 13, 1263-1269.
BODE, W., et al., 1994. THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY. EMBO JOURNAL, 13(6), p 1263-1269.
W. BODE, et al., “THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY”, EMBO JOURNAL, vol. 13, 1994, pp. 1263-1269.
BODE, W., REINEMER, P., HUBER, R., KLEINE, T., SCHNIERER, S., Tschesche, H.: THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY. EMBO JOURNAL. 13, 1263-1269 (1994).
BODE, W, REINEMER, P, HUBER, R, KLEINE, T, SCHNIERER, S, and Tschesche, Harald. “THE X-RAY CRYSTAL-STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE-ANALOG REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY”. EMBO JOURNAL 13.6 (1994): 1263-1269.

134 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Zhang D, Botos I, Gomis-Rüth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF., Proc Natl Acad Sci U S A 91(18), 1994
PMID: 8078901
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
Zinc content of the Bacillus anthracis lethal factor.
Kochi SK, Schiavo G, Mock M, Montecucco C., FEMS Microbiol Lett 124(3), 1994
PMID: 7851740
Structure-based drug design.
Colman PM., Curr Opin Struct Biol 4(6), 1994
PMID: 7712290

39 References

Daten bereitgestellt von Europe PubMed Central.

Sequence specificities of human fibroblast and neutrophil collagenases.
Netzel-Arnett S, Fields GB, Birkedal-Hansen H, Van Wart HE, Fields G., J. Biol. Chem. 266(11), 1991
PMID: 1849891
Vertebrate collagenase inhibitor. II. Tetrapeptidyl hydroxamic acids.
Odake S, Okayama T, Obata M, Morikawa T, Hattori S, Hori H, Nagai Y., Chem. Pharm. Bull. 39(6), 1991
PMID: 1657422
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
A comparison of the heme binding pocket in globins and cytochrome b5.
Rossmann MG, Argos P., J. Biol. Chem. 250(18), 1975
PMID: 1165251
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
On the size of the active site in proteases. I. Papain.
Schechter I, Berger A., Biochem. Biophys. Res. Commun. 27(2), 1967
PMID: 6035483
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
Generation of collagenase-resistant collagen by site-directed mutagenesis of murine pro alpha 1(I) collagen gene.
Wu H, Byrne MH, Stacey A, Goldring MB, Birkhead JR, Jaenisch R, Krane SM., Proc. Natl. Acad. Sci. U.S.A. 87(15), 1990
PMID: 2165607

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