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 ORCID: https://orcid.org/0000-0002-3965-9924, 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

Full text not available from this repository.

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:	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:	27 Oct 2022 10:13
URI:	https://orca.cardiff.ac.uk/id/eprint/69340

Citation Data

Cited 33 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item