FEBS Letters | |
The C‐terminal domains of TACE weaken the inhibitory action of N‐TIMP‐3 | |
Maskos, Klaus3  Becherer, J.David4  Amour, Augustin2  Murphy, Gillian1  Dodds, Philippa1  Lee, Meng-Huee1  Knäuper, Vera1  Verma, Vandana1  | |
[1] School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK;Glaxo Smith Kline, Stevenage, Herts SG1 2NY, UK;Max-Planck Institut für Biochemie, D-82152 Martinsried, Germany;Glaxo Smith Kline Research and Development Inc., 5 Moore Drive, Research Triangle Park, NC 27709, USA | |
关键词: N-TIMP-3; TACE-cat; TACE-long; Binding affinity; Association rate constants; TIMP-3; tissue inhibitor of metalloproteinases-3; TNF-α; tumor necrosis factor-α; TACE; tumor necrosis factor-α converting enzyme; ADAM-TS; ADAM proteinase with thrombospondin domains; Mca; (7-methoxycoumarin-4-yl)acetyl; Dnp; 2; 4-dinitrophenyl; | |
DOI : 10.1016/S0014-5793(02)02776-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Tumor necrosis factor-α converting enzyme (TACE) is an ADAM ( isintegrin nd etalloproteinases) 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.
【 授权许可】
Unknown
【 预 览 】
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