Entropy-driven cAMP-dependent allosteric control of inhibitory interactions in exchange proteins directly activated by cAMP

Journal of Biological Chemistry

Volumn 283, Issue 28, 2008, Pages 19691-19703

  Das, Rahul ^a   Mazhab Jafari, Mohammad T ^a   Chowdhury, Somenath ^a   SilDas, Soumita ^a   Selvaratnam, Rajeevan ^a   Melacini, Giuseppe ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; ELECTRIC LOAD MANAGEMENT; LAWS AND LEGISLATION; MODULATION; NUCLEIC ACIDS; PROTEINS;

ACTIVE STATES; ALLOSTERIC CONTROLS; BINDING DOMAINS; CATALYTIC CORES; CATALYTIC DOMAINS; COMPARATIVE ANALYSIS; CRITICAL DETERMINANTS; DYNAMIC FEATURES; DYNAMIC MODULATIONS; DYNAMIC PROFILES; EXCHANGE FACTORS; EXCHANGE PROTEINS; GTPASES; GUANINE NUCLEOTIDES; INHIBITORY INTERACTIONS; N TERMINUSES; PHOSPHOROTHIOATE; REGULATORY REGIONS; SALT BRIDGES; SECOND MESSENGERS;

FETAL MONITORING;

ANTIPORTER; CORE PROTEIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; EXCHANGE PROTEIN DIRECTLY ACTIVATED CYCLIC AMP; PHOSPHOROTHIOIC ACID; REGULATOR PROTEIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RAP PROTEIN; RAP1 PROTEIN; RAP2A PROTEIN, HUMAN; RAPGEF3 PROTEIN, HUMAN;

ALLOSTERISM; ALPHA HELIX; ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMICAL BOND; ENTROPY; ENZYME ACTIVATION; GENE MAPPING; GENETIC LINKAGE; MOLECULAR DYNAMICS; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SECOND MESSENGER;

EUKARYOTA;

ALLOSTERIC REGULATION; CYCLIC AMP; ENTROPY; GUANINE NUCLEOTIDE EXCHANGE FACTORS; HUMANS; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RAP GTP-BINDING PROTEINS; RAP1 GTP-BINDING PROTEINS; SECOND MESSENGER SYSTEMS;

EID: 50349092827     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M802164200     Document Type: Article

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