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Title: Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation.
Authors: Williamson, RA
Carr, MD
Frenkiel, TA
Feeney, J
Freedman, RB
First Published: 11-Nov-1997
Citation: BIOCHEMISTRY, 1997, 36 (45), pp. 13882-13889
Abstract: Changes in the NMR chemical shift of backbone amide nuclei (1H and 15N) 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-1 (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.
DOI Link: 10.1021/bi9712091
ISSN: 0006-2960
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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