Journal
FEBS LETTERS
Volume 520, Issue 1-3, Pages 102-106Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02776-X
Keywords
N-TIMP-3; TACE-cat; TACE-long; binding affinity; association rate constants
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available