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The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3

Lee, Meng-Huee, Verma, Vandana, Maskos, Klaus, Becherer, J. David, Knauper, Vera, Dodds, Philippa, Amour, Augustin and Murphy, Gillian 2002. The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. FEBS Letters 520 (1-3) , pp. 102-106. 10.1016/S0014-5793(02)02776-X

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Abstract

Tumor necrosis factor-α converting enzyme (TACE) is an ADAM (Math Eq Math Eqisintegrin Math Eqnd Math Eqetalloproteinases) 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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > Q Science (General)
Uncontrolled Keywords: N-TIMP-3; TACE-cat; TACE-long; Binding affinity; Association rate constants.
Publisher: Elsevier
ISSN: 0014-5793
Last Modified: 16 Jan 2019 14:57
URI: http://orca.cf.ac.uk/id/eprint/69340

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