Report

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

See allHide authors and affiliations

Science  04 Jun 1999:
Vol. 284, Issue 5420, pp. 1667-1670
DOI: 10.1126/science.284.5420.1667

You are currently viewing the abstract.

View Full Text

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.

  • * To whom correspondence should be addressed. E-mail: gunter{at}alfa.mbb.ki.se (G.S.); karl.tryggvason{at}mbb.ki.se (K.T.).

View Full Text