Structural dynamics and energetics underlying allosteric inactivation of the cannabinoid receptor CB1

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 27, 2015, Pages 8469-8474

  Fay, Jonathan F ^a   Farrens, David L ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

Allosteric; Biased signaling; CB1; GPCR; Protein dynamics

Indexed keywords

4 (1,1 DIMETHYLHEPTYL) 1',2',3',4',5',6' HEXAHYDRO 2,3' DIHYDROXY 6' (3 HYDROXYPROPYL)BIPHENYL; CANNABINOID 1 RECEPTOR; CANNABINOID 1 RECEPTOR ANTAGONIST; FLUORESCENT DYE; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; ORG 27569; RIMONABANT; TRANSMEMBRANE PROTEIN HELIX 6; TRANSMEMBRANE PROTEIN HELIX 8; UNCLASSIFIED DRUG; 3-(2-HYDROXY-4-(1,1-DIMETHYLHEPTYL)PHENYL)-4-(3-HYDROXYPROPYL)CYCLOHEXANOL; 5-CHLORO-3-ETHYL-1H-INDOLE-2-CARBOXYLIC ACID (2-(4-PIPERIDIN-1-YL-PHENYL)ETHYL)AMIDE; CANNABINOID RECEPTOR AGONIST; CANNABINOID RECEPTOR ANTAGONIST; CYCLOHEXANOL DERIVATIVE; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); INDOLE DERIVATIVE; PIPERIDINE DERIVATIVE; PYRAZOLE DERIVATIVE;

AGONIST; ALLOSTERISM; ARTICLE; COMPETITIVE INHIBITION; CONFORMATIONAL TRANSITION; COS 1 CELL LINE; DRUG CONFORMATION; DRUG RECEPTOR BINDING; ISOMERIZATION; PRIORITY JOURNAL; WESTERN BLOTTING; ALGORITHM; ANIMAL; BINDING COMPETITION; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; CHLOROCEBUS AETHIOPS; GENETICS; HUMAN; KINETICS; METABOLISM; MUTATION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RADIOASSAY;

CANNABIS SATIVA;

ALGORITHMS; ANIMALS; BINDING, COMPETITIVE; CANNABINOID RECEPTOR AGONISTS; CANNABINOID RECEPTOR ANTAGONISTS; CERCOPITHECUS AETHIOPS; COS CELLS; CYCLOHEXANOLS; GUANOSINE 5'-O-(3-THIOTRIPHOSPHATE); HUMANS; INDOLES; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MUTATION; PIPERIDINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRAZOLES; RADIOLIGAND ASSAY; RECEPTOR, CANNABINOID, CB1;

EID: 84936817683     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1500895112     Document Type: Article

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