Dynamics of cleft closure of the GluA2 ligand-binding domain in the presence of full and partial agonists revealed by hydrogen-deuterium exchange

Journal of Biological Chemistry

Volumn 288, Issue 38, 2013, Pages 27658-27666

  Ahmed, Ahmed H ^a   Ptak, Christopher P ^a   Fenwick, Michael K ^a   Hsieh, Ching Lin ^a   Weiland, Gregory A ^a   Oswald, Robert E ^a  

^a Department of Obstetrics Gynecology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA-RECEPTOR; BINDING DOMAIN; CHANNEL ACTIVATION; CONFORMATIONAL TRANSITIONS; EXCITATORY NEUROTRANSMISSION; HYDROGEN-DEUTERIUM EXCHANGE; ION CHANNEL; LIGAND BINDING DOMAIN;

DEUTERIUM; LIGANDS; STABILIZATION;

HYDROGEN BONDS;

GLUTAMATE RECEPTOR; GLUTAMATE RECEPTOR AGONIST; SERINE; TRYPTOPHAN;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; DESENSITIZATION; DEUTERIUM HYDROGEN EXCHANGE; GENE MUTATION; HUMAN; HYDROGEN BOND; LIGAND BINDING; NEUROTRANSMISSION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARTIAL AGONISM; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY;

GLUTAMATE RECEPTORS; HYDROGEN-DEUTERIUM EXCHANGE; IONOTROPIC GLUTAMATE RECEPTORS (AMPA, NMDA); MEMBRANE PROTEINS; NEUROTRANSMITTER RECEPTORS; NMR; WILLARDIINE;

ANIMALS; DEUTERIUM EXCHANGE MEASUREMENT; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; MOLECULAR DYNAMICS SIMULATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, AMPA; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84884558766     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.495564     Document Type: Article

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