The conformational activation of antithrombin. A 2.85-Å structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions

Journal of Biological Chemistry

Volumn 275, Issue 20, 2000, Pages 15377-15383

  Huntington, James A ^a   McCoy, Airlie ^a   Belzar, Klara J ^a   Pei, Xue Y ^a   Gettins, Peter G W ^b   Carrell, Robin W ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; GLUTAMINE; HEPARIN BINDING PROTEIN; PROTEINASE; SERINE PROTEINASE INHIBITOR;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME CONFORMATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTITHROMBINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ELECTROSTATICS; FACTOR XA; FLUORESCEIN; GLUTAMIC ACID; HEPARIN; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 0034685780     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.20.15377     Document Type: Article

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