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MMP–TIMP interaction depends on residue 2 in TIMP‐4
Author(s) -
Stratmann Bernd,
Farr Martin,
Tschesche Harald
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02987-8
Subject(s) - matrix metalloproteinase , residue (chemistry) , extracellular matrix , chemistry , microbiology and biotechnology , extracellular , biophysics , biochemistry , biology
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 (Ser 2 ) 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.