- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.m211793200
-
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2003
Journal article
Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors.
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