Linked Life Data

9374866

Source:http://linkedlifedata.com/resource/pubmed/id/9374866

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
1997-12-8
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13882-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation.
pubmed:affiliation
Research School of Biosciences, University of Kent, Canterbury, U.K. r.a.williamson@ukc.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't