A ligand channel through the G protein coupled receptor opsin

The G protein coupled receptor rhodopsin contains a pocket within its seven-transmembrane helix (TM) structure, which bears the inactivating 11-cis-retinal bound by a protonated Schiff-base to Lys296 in TM7. Light-induced 11-cis-/all-trans-isomerization leads to the Schiff-base deprotonated active M...

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Veröffentlicht in:	PloS one 2009-02, Vol.4 (2), p.e4382-e4382
Hauptverfasser:	Hildebrand, Peter W, Scheerer, Patrick, Park, Jung Hee, Choe, Hui-Woog, Piechnick, Ronny, Ernst, Oliver P, Hofmann, Klaus Peter, Heck, Martin
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Biochemistry/Bioinformatics Biochemistry/Drug Discovery Biochemistry/Theory and Simulation Biophysics/Biomacromolecule-Ligand Interactions Biophysics/Membrane Proteins and Energy Transduction Biophysics/Theory and Simulation Computational Biology Computer applications Constrictions Crystal structure Elbow Elbow (anatomy) G proteins Hostages Hydrophobicity Ionone Isomerism Isomerization Ligands Lysine Lysine - metabolism Models, Molecular Molecular conformation Molecular docking Molecular Sequence Data Photoreceptors Protein Structure, Secondary Proteins Retina Retinaldehyde Retinaldehyde - chemistry Rhodopsin Rhodopsin - chemistry Rhodopsin - metabolism Tissue engineering
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