Lipid protein interactions couple protonation to conformation in a conserved cytosolic domain of G protein-coupled receptors

Journal of Biological Chemistry

Volumn 284, Issue 42, 2009, Pages 28801-28809

  Madathil, Sineej ^a   Fahmy, Karim ^a  

^a INSTITUTE OF ION BEAM PHYSICS AND MATERIALS RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE RHODOPSIN; CLASS I; COUPLING MECHANISM; COVALENTLY BOUND; CYTOSOLIC; CYTOSOLIC DOMAINS; FOERSTER RESONANCE ENERGY TRANSFERS; FREE ENTHALPY; FUNCTIONAL MODULES; G PROTEIN; G PROTEIN COUPLED RECEPTORS; INTERHELICAL CONTACTS; LIPID-PROTEIN INTERACTIONS; PHOTO-ACTIVATED; SIDE CHAINS; SPECIFIC INTERACTION; TRANSMEMBRANE HELICES; TRANSMEMBRANE SEGMENTS;

ENERGY TRANSFER; LIGANDS;

PROTONATION;

G PROTEIN COUPLED RECEPTOR; RHODOPSIN;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOSOL; ENTHALPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; INFRARED SPECTROSCOPY; LIPID BILAYER; NONHUMAN; PHOTOACTIVATION; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT;

AMINO ACID MOTIFS; ANIMALS; CATTLE; CYTOSOL; HYDROGEN-ION CONCENTRATION; LIGANDS; LIPIDS; MICELLES; PHOTORECEPTOR CELLS, VERTEBRATE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTONS; RECEPTORS, G-PROTEIN-COUPLED; RHODOPSIN; SPECTROMETRY, FLUORESCENCE;

BOVINAE;

EID: 70350752268     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.002030     Document Type: Article

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