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Letters to Nature

Nature 389, 77-81 (4 September 1997) | doi:10.1038/37995; Received 30 April 1997; Accepted 13 June 1997

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

Franz-Xaver Gomis-R¨th1,5, Klaus Maskos1,5, Michael Betz1, Andreas Bergner1, Robert Huber1, Ko Suzuki2, Naoki Yoshida2, Hideaki Nagase2, Keith Brew3, Gleb P. Bourenkov4, Hans Bartunik4 & Wolfram Bode1

  1. Max-Planck-Institut für Biochemie, Abteilung für Strukturforschung, D-82152 Martinsried, Germany
  2. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas66160, USA
  3. Department of Biochemistry and Molecular Biology, University of Miami, School of Medicine, Miami, Florida33101, USA
  4. AG Proteindynamik MPG-ASMB, c/o DESY, D-22603 Hamburg, Germany
  5. These authors contributed equally to this work.

Correspondence to: Correspondence and requests for materials should be addressed to W.B. (e-mail:Email: bode@biochem.mpg.de).The coordinates have been deposited at the Protein Data Bank (accession no. PDB ID code IUEA).

Matrix metalloproteinases (MMPs) are zinc endopeptidases that are required for the degradation of extracellular matrix components during normal embryo development, morphogenesis and tissue remodelling1. Their proteolytic activities are precisely regulated by endogenous tissue inhibitors of metalloproteinases (TIMPs)1, 2, 3, 4, 5.