Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation

Williamson, R.A. and Carr, M.D. and Frenkiel, T.A. and Feeney, J. and Freedman, R.B. (1997) Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry, 36 (45). pp. 13882-13889. ISSN 0006-2960. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1021/bi9712091

Abstract

Changes in the NMR chemical shift of backbone amide nuclei (H-1 and N-15) have been used to map the matrix metalloproteinase (MMP) binding site on the N-terminal domain of the tissue inhibitor of metalloproteinase-2 (N-TIMP-2). Amide chemical shift changes were measured on formation of a stable complex with the catalytic domain of stromelysin-l (N-MMP-3). Residues with significantly shifted amide signals mapped specifically to a broad site covering one face of the molecule. This site (the MMP binding site) consists primarily of residues 1-11, 27-41, 68-73, 87-90, and 97-104. The site overlaps with the OB-fold binding site seen in other proteins that share the same five-stranded beta-barrel topology. Sequence conservation data and recent site-directed mutagenesis studies are discussed in relation to the MMP binding site identified in this work.

Item Type: Article
Additional information: 0006-2960 (Print) Journal Article Research Support, Non-U.S. Gov't
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Cell & Developmental Biology Group
Depositing User: T.J. Sango
Date Deposited: 17 Apr 2009 11:57
Last Modified: 20 Jul 2009 16:53
Resource URI: http://kar.kent.ac.uk/id/eprint/18046 (The current URI for this page, for reference purposes)
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