The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function

Journal of Biological Chemistry

Volumn 271, Issue 34, 1996, Pages 20365-20374

  Paul Mould, A ^a   Akiyama, Steven K ^b   Humphries, Martin J ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; INTEGRIN; LIGAND; MONOCLONAL ANTIBODY; ARGINYL-GLYCYL-ASPARTIC ACID; ARGINYLGLYCYLASPARTIC ACID; BETA1 INTEGRIN; FIBRONECTIN RECEPTOR; OLIGOPEPTIDE; PEPTIDE;

ALLOSTERISM; ANTIGEN BINDING; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; HUMAN; HUMAN TISSUE; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; RECEPTOR OCCUPANCY; AMINO ACID SEQUENCE; ANIMAL; ANTIGEN ANTIBODY REACTION; BINDING COMPETITION; CHEMISTRY; IMMUNOLOGY; MOLECULAR GENETICS; RAT;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, MONOCLONAL; ANTIGEN-ANTIBODY REACTIONS; ANTIGENS, CD29; BINDING, COMPETITIVE; EPITOPES; HUMANS; LIGANDS; MOLECULAR SEQUENCE DATA; OLIGOPEPTIDES; PEPTIDES; RATS; RECEPTORS, FIBRONECTIN;

EID: 0029664954     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.34.20365     Document Type: Article

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