期刊
FEBS LETTERS
卷 520, 期 1-3, 页码 102-106出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02776-X
关键词
N-TIMP-3; TACE-cat; TACE-long; binding affinity; association rate constants
Tumor necrosis factor-alpha converting enzyme (TACE) is an ADAM (a disintegrin and metalloproteinases) that comprises an active catalytic domain and several C-terminal domains. We compare the binding affinity and association rate constants of the N-terminal domain form of wild-type tissue inhibitor of metalloproteinase (TIMP-3; N-TIMP-3) and its mutants against full-length recombinant TACE and the truncated form of its catalytic domain. We show that the C-terminal domains of TACE substantially weaken the inhibitory action of N-TIMP-3. Further probing with hydroxamate inhibitors indicates that both forms of TACE have similar active site configurations. Our findings highlight the potential role of the C-terminal domains of ADAM proteinases in influencing TIMP interactions. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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