The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure.

By T. Okada, M. Sugihara, A. Bondar, Marcus Elstner, P. Entel, V. Buss. Journal of Molecular Biology, 2004

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Assessment and Challenges of Ligand Docking into Comparative Models of G-Protein Coupled Receptors (2013, background): “This includes the following G-protein coupled receptors: rhodopsin [14], b 1-adrenergic [15], b 2-adrenergic [16], A2A adenosine [17], CXCR4 chemokine [18], dopamine D3 [19], histamine H1 [20], S1P1 sphingosine 1-phosphate [21], M2 muscarinc acetylcholine [22], M3 muscarinic acetylecholine [23],…”
Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions (2012, background): “S6A), and positions of four of the ten water molecules are similar to those found in bovine rhodopsin (PDB ID 1U19) (22) (fig.”
Conical intersection dynamics of the primary photoisomerization event in vision (2010, background): “These calculations imply highly constrained dynamics of the retinal chromophore on the excited state prior to isomerization, restricted almost exclusively to the C9 = C10 − C11 = C12 region of the chromophore, an interpretation which is consistent with the highest resolution crystal structure for bo”
Structure-Function of the G-protein-Coupled Receptor Superfamily (2012, background): “Several GPCRs, such as rhodopsin (9, 14, 15, 17, 18, 38, 39), β2AR (21, 22, 27, 40, 41),β1AR (13, 42, 43), A2AAR (19, 20, 44, 45) and CXCR4 (33), have been co-crystallized in complexes with different ligands, in different crystal forms or using different approaches to receptor stabilization and crys”