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Volumn 275, Issue 49, 2000, Pages 38762-38767
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An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
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Author keywords
[No Author keywords available]
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Indexed keywords
GLYCINE;
INTEGRIN;
ISOLEUCINE;
LIGAND;
VON WILLEBRAND FACTOR;
ALLOSTERISM;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
BINDING AFFINITY;
CARBOXY TERMINAL SEQUENCE;
CELL STIMULATION;
CRYSTAL STRUCTURE;
HYDROPHOBICITY;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DOMAIN;
SIGNAL TRANSDUCTION;
STRUCTURE ACTIVITY RELATION;
ALLOSTERIC REGULATION;
ALLOSTERIC SITE;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ANTIGENS, CD;
BINDING SITES;
CRYSTALLOGRAPHY, X-RAY;
HUMANS;
ISOLEUCINE;
MACROPHAGE-1 ANTIGEN;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
PEPTIDE FRAGMENTS;
PROTEIN CONFORMATION;
RECOMBINANT PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE DELETION;
SEQUENCE HOMOLOGY, AMINO ACID;
SOLUTIONS;
VON WILLEBRAND FACTOR;
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EID: 0034624058
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.C000563200 Document Type: Article |
Times cited : (130)
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References (37)
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