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Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.

Abstract:

Studies of the structural basis of the interactions of tissue inhibitors of metalloproteinases (TIMPs) and matrix metalloproteinases (MMPs) may provide clues for designing MMP-specific inhibitors. In this paper we report combinations of mutations in the major MMP-binding region that enhance the specificity of N-TIMP-1. Mutants with substitutions for residues 4 and 68 were characterized and combined with previously studied Thr(2) mutations to generate mutants with improved selectivity or bindi...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m211793200

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Institution:
University of Oxford
Department:
Oxford, MSD, NDORMS
Journal:
The Journal of biological chemistry
Volume:
278
Issue:
11
Pages:
9831-9834
Publication date:
2003-03-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:9b17e628-24fb-404a-aeb0-722b4bf89f20
Source identifiers:
226993
Local pid:
pubs:226993

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