MMP–TIMP interaction depends on residue 2 in TIMP‐4

FEBS Letters

Stratmann, Bernd¹  Tschesche, Harald¹  Farr, Martin¹ 

[1] University of Bielefeld, Faculty of Chemistry, Biochemistry I, Universitätsstraße 25, D-33615 Bielefeld, Germany

关键词: Matrix metalloproteinase;    Tissue inhibitor of metalloproteinase;    Matrix metalloproteinase–tissue inhibitor of metalloproteinase interaction;    Tissue inhibitor of metalloproteinase specifity;    TIMP;    tissue inhibitor of metalloproteinase;    MMP;    matrix metalloproteinase;    cd;    catalytic domain;    id;    inhibitory domain;   

DOI  :  10.1016/S0014-5793(01)02987-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Extracellular matrix remodeling and degradation are of great importance in both physiological and pathological situations. Matrix metalloproteinases (MMPs) and their natural occurring inhibitors – tissue inhibitors of metalloproteinases (TIMPs) – are involved in matrix turnover. Among the TIMPs there is only little specificity for inhibiting individual MMPs. In this report we describe the mutational analysis of the interaction of human TIMP-4 with several MMPs. The effects of different substitutions of residue 2 (Ser²) in the inhibitory domain of TIMP-4 were determined by kinetic measurements. Size, charge and polarity of residue 2 in the TIMP structure are key factors in MMP inhibition.

【 授权许可】

Unknown