Subscribe to Journal
Get full journal access for 1 year
only $3.90 per issue
All prices are NET prices.
VAT will be added later in the checkout.
Tax calculation will be finalised during checkout.
Rent or Buy article
Get time limited or full article access on ReadCube.
All prices are NET prices.
Nagase, H. in Zinc Metalloproteases in Health and Disease(ed. Hooper, N. M.) 153–204 (Taylor and Francis, London, (1996)).
Coussens, L. M. & Werb, Z. Matrix metalloproteinases and the development of cancer. Chem. Biol. 3, 895–904 (1996).
Green, J.et al. Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4. J. Biol. Chem. 271, 30375–30380 (1996).
Willenbrock, F. & Murphy, G. Structure–function relationships in the tissue inhibitors of metalloproteinases. Am. J. Resp. Crit. Care Med. 150, 5165–5170 (1994).
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).
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).
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).
Gooley, P. R.et al. NMR structure of inhibited catalytic domain of human stomelysin-1. Nature Struct. Biol. 1, 111–118 (1994).
Becker, J. W.et al. Stromelysin-1: Three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Prot. Sci. 4, 1966–1976 (1995).
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).
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).
Murzin, A. G. OB-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12, 861–867 (1993).
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).
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).
Huovila, A. P., Ilmeida, E. A. C. & White, J. M. ADAMs and cell fusion. Curr. Opin. Cell Biol. 8, 692–699 (1996).
Stöcker, W.et al. The metzincins: Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823–840 (1995).
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).
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).
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).
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).
Black, R. A.et al. Ametalloproteinase disintegrin that releases tumour-necrosis factor-α from cells. Nature 385, 729–733 (1997).
Moss, M. L.et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385, 733–736 (1997).
Otwinowski, Z. & Minor, W. DENZO: A Film Processing for Macromolecular Crystallography(Yale University, New Haven, CT, (1993)).
Navaza, J. AMoRe: an automated package for molecular replacement. Acta crystallogr. A 50, 157–163 (1994).
Otwinowski, Z. in Isomorphous Replacement and Anomalous Scattering, Daresbury study weekend proceedings(SERC Daresbury Laboratory, Warrington, (1991)).
Cowtan, K. Joint CCP4 ESF-EACBM Newsletter on Protein Crystallography Vol. 31(1994).
Roussel, A. & Cambilleau, C. Turbo-Frodo in Silicon Graphics Geometry, Partners Directory(Silicon Graphics, Mountain View, CA, (1989)).
Brünger, A. T. Crystallographic phasing and refinement of macromolecules. Curr. Opin. Struct. Biol 1, 1016–1022 (1991).
Nicholls, A., Bharadwaj, R. & Honig, B. Grasp–graphical representation and analysis of surface properties. Biophys. J. 64, 166 (1993).
We thank M. Braun for help with crystallization, M. T. Stubbs for reading the manuscript, and A. Lebedev and E. H. Panepucci for help with molecular replacement. This work was supported by the SFB469, the Human Capital and Mobility, and the Biotechnology programs of the European Union, the Fonds der Chemischen Industrie, the BMBF, and the NIH.
About this article
Cite this article
Gomis-R¨th, FX., Maskos, K., Betz, M. et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77–81 (1997). https://doi.org/10.1038/37995
Structural characterisation of inhibitory and non-inhibitory MMP-9–TIMP-1 complexes and implications for regulatory mechanisms of MMP-9
Scientific Reports (2021)
Establishment of Structure-Function Relationship of Tissue Inhibitor of Metalloproteinase-1 for Its Interaction with CD63: Implication for Cancer Therapy
Scientific Reports (2020)
Calcified Tissue International (2020)
Cancer and Metastasis Reviews (2019)
Cellular and Molecular Life Sciences (2019)