The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.
作者： Frances Willenbrock , Thomas Crabbe , Patrick M. Slocombe , Chris W. Sutton , Andrew J. P. Docherty
DOI: 10.1021/BI00067A023
关键词:
摘要: The cloning and expression of the full-length tissue inhibitor metalloproteinase 2 (TIMP-2), delta 187-194TIMP-2, 128-194TIMP-2 purification these inhibitors a cleaved version TIMP-2 lacking nine C-terminal amino acids (delta 186-194TIMP-2) are described. mechanism inhibition gelatinase A by TIMPs was investigated comparing kinetics association TIMP-1, TIMP-2, deletions, mutants both which consisted N-terminal domain only. inhibited rapidly with constants 3.2 x 10(6) M-1 s-1 for TIMP-1 2.1 10(7) at I = 0.2. peptide is proposed to exist as an exposed "tail" responsible binding progelatinase increasing rate active through electrostatic interactions enzyme. domains participate in low-affinity increase factor about 100 cases.
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