Ligand binding to anion-binding exosites regulates conformational properties of thrombin

Journal of Biological Chemistry

Volumn 288, Issue 12, 2013, Pages 8667-8678

  Malovichko, Marina V ^a   Sabo, T Michael ^a,b   Maurer, Muriel C ^a  

^a UNIVERSITY OF LOUISVILLE   (United States)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-COAGULATION; CONFORMATIONAL PROPERTIES; CURRENT PROJECTS; HYDROGEN-DEUTERIUM EXCHANGE; LIGAND COMPLEXES; LONG RANGE EFFECTS; MALDI-TOF MASS SPECTROMETRY; PLATELET ACTIVATION;

AMINO ACIDS; COMPLEXATION; KETONES; LIGANDS; MASS SPECTROMETRY;

ENZYMES;

DEXTRO PHENYLALANYLPROLYLARGINYL CHLOROMETHYL KETONE; HIRUDIN; PROTEINASE ACTIVATED RECEPTOR 1; PROTEINASE ACTIVATED RECEPTOR 3; THROMBIN;

ANION BINDING EXOSITE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME STRUCTURE; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN TARGETING;

AMINO ACID CHLOROMETHYL KETONES; ANIMALS; ANIONS; BINDING SITES; CATALYTIC DOMAIN; CATTLE; DEUTERIUM EXCHANGE MEASUREMENT; FIBRINOGEN; HIRUDINS; LIGANDS; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN BINDING; RECEPTORS, THROMBIN; THROMBIN;

EID: 84875430212     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.410829     Document Type: Article

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