Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

Nature

Volumn 389, Issue 6646, 1997, Pages 77-81

  Gomis Rüth, Franz Xaver ^a   Maskos, Klaus ^a   Betz, Michael ^a   Bergner, Andreas ^a   Huber, Robert ^a   Suzuki, Ko ^b   Yoshida, Naoki ^b   Nagase, Hideaki ^b   Brew, Keith ^c   Bourenkov, Gleb P ^d   Bartunlk, Hans ^d   Bode, Wolfram ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

^d MAX PLANCK UNIT FOR STRUCTURAL MOLECULAR BIOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE INHIBITOR; STROMELYSIN; TISSUE INHIBITOR OF METALLOPROTEINASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME INHIBITION; ESCHERICHIA COLI; EXTRACELLULAR MATRIX; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; STRUCTURE ACTIVITY RELATION;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; MATRIX METALLOPROTEINASE 3; MODELS, MOLECULAR; PROTEASE INHIBITORS; PROTEIN CONFORMATION; TISSUE INHIBITOR OF METALLOPROTEINASES;

ESCHERICHIA COLI;

EID: 1842377505     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/37995     Document Type: Article

References (30)

1. Nagase, H. in Zinc Metalloproteases in Health and Disease (ed. Hooper, N. M.) 153-204 (Taylor and Francis, London, 1996).
2. Coussens, L. M. & Werb, Z. Matrix metalloproteinases and the development of cancer. Chem. Biol. 3, 895-904 (1996).
3. Green, J. et al. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J. Biol. Chem. 271, 30375-30380 (1996).
4. Willenbrock, F. & Murphy, G. Structure-function relationships in the tissue inhibitors of metalloproteinases. Am. J. Resp. Crit. Care Med. 150, 5165-5170 (1994).
5. Docherty, A. J. P. et al. Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity. Nature 318, 66-69 (1985).
6. Murphy, G. et al. The N-terminal domain of human tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry 30, 8097-8102 (1991).
7. Huang, W. et al. Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinase-1 (TIMP-1) expressed at high yield in E. coli. FEBS Lett. 384, 155-161 (1996).
8. Williamson, R. A. et al. Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family. Biochemistry 33, 11745-11759 (1994).
9. Gooley, P. R. et al. NMR structure of inhibited catalytic domain of human stomelysin-1. Nature Struct. Biol. 1, 111-118 (1994).
10. Becker, J. W. et al. Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Prof. Sci. 4, 1966-1976 (1995).
11. Dhanaraj, V. et al. X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily. Structure 4, 375-386 (1996).
12. Li, J.-Y. et al. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed β-propeller Structure 3, 541-549 (1995).
13. Murzin, A. G. OB-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12, 861-867 (1993).
14. Grams, F. et al. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design. Eur. J. Biochem. 228, 830-841 (1995).
15. Will, H., Atkinson, S. J., Butler, G. S., Smyth, B. & Murphy, G. The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autocatalytic activation. J. Biol. Chem. 271, 17119-17123 (1996).
16. Huovila, A. P., Ilmeida, E. A. C. & White, J. M. ADAMs and cell fusion. Curr. Opin. Cell Biol. 8, 692- 699 (1996).
17. Stöcker, W. et al. The metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (couagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840 (1995).
18. Kessler, E., Takahara, K., Biniaminov, L., Brusel, M. & Greenspan, D. S. Bone morphogenetic protein- 1: The type I procollagen C-proteinase. Science 271, 360-362 (1996).
19. Baumann, U., Wu, S., Flaherty, K. M. & McKay, D. B. Three-dimensional structure of the alkaline proteae of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel β roll motif. EMBO J. 12, 3357-3364 (1993).
20. Bode, W., Gomis-Rüth, F. X., Huber, R., Zwilling, R. & Stöcker, W. Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-166 (1992).
21. Gomis-Rüth, F. X., Kress, L. F. & Bode, W. First structure of a snake venom metalloproteinase: prototype for matrix metalloproteinases/collagenases. EMBO J. 12, 4151-4157 (1993).
22. Black, R. A. et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729-733 (1997).
23. Moss, M. L. et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733-736 (1997).
24. Otwinowski, Z. & Minor, W. DENZO: A Film Processing for Macromolecular Crystallography (Yale University, New Haven, CT, 1993).
25. Navaza, J. AMoRe: an automated package for molecular replacement. Acta crystallogr. A 50, 157-163 (1994).
26. Otwinowski, Z. in Isomorphous Replacement and Anomalous Scattering, Daresbury study weekend proceedings (SERC Daresbury Laboratory, Warrington, 1991).
27. Cowtan, K. Joint CCP4 ESF-EACBM Newsletter on Protein Crystallography Vol. 31 (1994).
28. Roussel, A. & Cambilleau, C. Turbo-Frodo in Silicon Graphics Geometry, Partners Directory (Silicon Graphics, Mountain View, CA, 1989).
29. Brünger, A. T. Crystallographic phasing and refinement of macromolecules. Curr. Opin. Struct. Biol 1, 1016-1022 (1991).
30. Nicholls, A., Bharadwaj, R. & Honig, B. Grasp - graphical representation and analysis of surface properties. Biophys. J. 64, 166 (1993).