Residues Tyr253 and Glu255 in strand 3 of β-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa

Journal of Biological Chemistry

Volumn 281, Issue 19, 2006, Pages 13424-13432

  Izaguirre, Gonzalo ^a   Olson, Steven T ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOCHEMISTRY; CONFORMATIONS; ENZYME INHIBITION; MUTAGENESIS;

ANTITHROMBIN; CONFORMATIONAL ACTIVATION; HEPARIN ACTIVATION;

DRUG PRODUCTS;

ALPHA 1 ANTITRYPSIN; ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 9A; GLUTAMIC ACID; GLUTAMINE; HEPARIN; TYROSINE; ANTITHROMBIN III; THROMBIN;

ANIMAL CELL; ARTICLE; BETA SHEET; BINDING AFFINITY; CHIMERA; CONTROLLED STUDY; GENE MUTATION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; WILD TYPE; AMINO ACID SEQUENCE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; GENETICS; HUMAN; KINETICS; METABOLISM; MUTATION; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE;

VERTEBRATA;

AMINO ACID SEQUENCE; ANTITHROMBIN III; BINDING SITES; FACTOR IXA; FACTOR XA; GLUTAMIC ACID; HEPARIN; HUMANS; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; THROMBIN; TYROSINE;

EID: 33744951403     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M600415200     Document Type: Article

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