Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed

被引：462

作者：

Morgunova, E

Tuuttila, A

Bergmann, U

Isupov, M

Lindqvist, Y

Schneider, G ^{[1
]}

Tryggvason, K

机构：

[1] Karolinska Inst, Dept Med Biochem & Biophys, Div Matrix Biol, Stockholm, Sweden

[2] Karolinska Inst, Dept Med Biochem & Biophys, Div Mol Struct Biol, Stockholm, Sweden

[3] Univ Exeter, Sch Chem, Exeter EX4 4QJ, Devon, England

[4] Univ Exeter, Sch Biol Sci, Exeter EX4 4QJ, Devon, England

来源：

SCIENCE | 1999年 / 284卷 / 5420期

关键词：

D O I：

10.1126/science.284.5420.1667

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1667 / 1670

页数：4

共 49 条

[1] Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes [J].