Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed-Reference-Cited by-同舟云学术

Structure of Human Pro-Matrix Metalloproteinase-2: Activation Mechanism Revealed

Published:1999-06-04 Issue:5420 Volume:284 Page:1667-1670
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Morgunova Ekaterina¹²,Tuuttila Ari¹,Bergmann Ulrich¹,Isupov Mikhail³,Lindqvist Ylva²,Schneider Gunter²,Tryggvason Karl¹

Affiliation:

1. Division of Matrix Biology, Department of Medical Biochemistry and Biophysics and

2. Division of Molecular Structural Biology, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.

3. Schools of Chemistry and Biological Sciences, University of Exeter, UK.

Abstract

Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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