An allosteric Ca2+ binding site on the β3-integrins that regulates the dissociation rate for RGD ligands

Journal of Biological Chemistry

Volumn 271, Issue 36, 1996, Pages 21745-21751

  Hu, Dana D ^a   Barbas III, Carlos F ^b   Smith, Jeffrey W ^a  

^a BURNHAM INSTITUTE   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; INTEGRIN; MAGNESIUM ION; ANTIBODY; ARGINYL GLYCYL ASPARTIC ACID DIRECTED CELL ADHESION RECEPTOR; ARGINYL-GLYCYL-ASPARTIC ACID; ARGINYL-GLYCYL-ASPARTIC ACID DIRECTED CELL ADHESION RECEPTOR; ARGINYLGLYCYLASPARTIC ACID; BETA3 INTEGRIN; CALCIUM; FIBRINOGEN RECEPTOR; IMMUNOGLOBULIN RECEPTOR; LEUKOCYTE ANTIGEN; MAGNESIUM; OLIGOPEPTIDE; RECEPTOR;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; BINDING KINETICS; BINDING SITE; CALCIUM BINDING; CELL ADHESION; COMPETITIVE INHIBITION; DISSOCIATION CONSTANT; EMBRYO; HUMAN; HUMAN CELL; HUMAN TISSUE; PRIORITY JOURNAL; PROTEIN BINDING; BINDING COMPETITION; CELL LINE; KINETICS; METABOLISM;

ALLOSTERIC SITE; ANTIBODIES; ANTIGENS, CD; BINDING, COMPETITIVE; CALCIUM; CELL ADHESION; CELL LINE; HUMANS; INTEGRIN BETA3; KINETICS; MAGNESIUM; OLIGOPEPTIDES; PLATELET MEMBRANE GLYCOPROTEINS; RECEPTORS, IMMUNOLOGIC; RECEPTORS, PEPTIDE;

EID: 0029664968     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.36.21745     Document Type: Article

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