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

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78365

Maskos,  K.
Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society;

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Lee, M. H., Verma, V., Maskos, K., Becherer, J. D., Knäuper, V., Dodds, P., et al. (2002). The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. FEBS Letters, 520(1-3), 102-106.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F06-B
Abstract
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.