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

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Figure 1: Stereo ribbon diagram of the complex formed between TIMP-1 (red) and the MMP-3 catalytic domain (blue).
Figure 2: Ribbon of TIMP-1 (red) shown together with the full side chains of some important residues and the disulphide connections.
Figure 3: Stereo view from the centre of TIMP-1, towards the active-site cleft of MMP-3, which is represented by a solid surface coloured according .
Figure 4: Stereo view of the section of the final 2.

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Acknowledgements

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.

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Author notes

  1. Franz-Xaver Gomis-R¨th and Klaus Maskos: These authors contributed equally to this work.

Authors and Affiliations

  1. Abteilung für Strukturforschung, Max-Planck-Institut für Biochemie, Martinsried, D-82152, Germany

    Franz-Xaver Gomis-R¨th, Klaus Maskos, Michael Betz, Andreas Bergner, Robert Huber & Wolfram Bode

  2. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, 66160, Kansas, USA

    Ko Suzuki, Naoki Yoshida & Hideaki Nagase

  3. Department of Biochemistry and Molecular Biology, University of Miami, School of Medicine, Miami, 33101, Florida, USA

    Keith Brew

  4. AG Proteindynamik MPG-ASMB, c/o DESY, Hamburg, D-22603, Germany

    Gleb P. Bourenkov & Hans Bartunik

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  1. Franz-Xaver Gomis-R¨th
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  2. Klaus Maskos
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  3. Michael Betz
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  8. Hideaki Nagase
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  12. Wolfram Bode
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Correspondence to Wolfram Bode.

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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

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