A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor.

By M. Hanson, Vadim Cherezov, Mark T. Griffith, Christopher B. Roth, Veli-Pekka Jaakola, E. Chien, Jeff Velasquez, P. Kuhn, Raymond C. Stevens. Structure, 2008

939 citations recorded by the source corpus.

Subfields: Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/9b7bf64ef8df832a1b1424374e03687f2c6bad59

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Citations in the corpus

Structure-Function of the G-protein-Coupled Receptor Superfamily (2012, background): “Several potential allosteric sites in GPCRs revealed by crystal structures have been reviewed previously (53), including a phosphate ion binding site in the extracellular subpocket of the histamine H1 structure (28), a cholesterol binding site in β2AR (40) and a ‘druggable’ extracellular extension o”
Computing Highly Correlated Positions Using Mutual Information and Graph Theory for G Protein-Coupled Receptors (2009, background): “GPCR crystal structures, available for rhodopsin and two subtypes of the b-adrenergic receptors (b-ARs), and computational models supported by biochemical and molecular pharmacological data suggest the presence of a common binding cavity, located within the TMs toward the extracellular side of the h”
Lifting the lid on GPCRs: the role of extracellular loops (2011, background): “carazolol, timolol, ICI 118551 and ‘compound 2’ (Cherezov et al., 2007; Hanson et al., 2008; Wacker et al., 2010) and a neutral antagonist alprenolol (Wacker et al.”