3D4S
Cholesterol bound form of human beta2 adrenergic receptor.
Summary for 3D4S
| Entry DOI | 10.2210/pdb3d4s/pdb |
| Related | 2RH1 |
| Descriptor | Beta-2 adrenergic receptor/T4-lysozyme chimera, (2S)-1-(tert-butylamino)-3-[(4-morpholin-4-yl-1,2,5-thiadiazol-3-yl)oxy]propan-2-ol, CHOLESTEROL, ... (5 entities in total) |
| Functional Keywords | gpcr, membrane protein, lysozyme, fusion, adrenergic, timolol, g-protein coupled receptor, glycoprotein, lipoprotein, palmitate, phosphoprotein, receptor, transducer, transmembrane, structural genomics, psi-2, protein structure initiative, accelerated technologies center for gene to 3d structure, atcg3d, gpcr network |
| Biological source | Homo sapiens More |
| Cellular location | Cell membrane ; Multi- pass membrane protein : P07550 |
| Total number of polymer chains | 1 |
| Total formula weight | 58117.27 |
| Authors | Hanson, M.A.,Cherezov, V.,Roth, C.B.,Griffith, M.T.,Jaakola, V.-P.,Chien, E.Y.T.,Velasquez, J.,Kuhn, P.,Stevens, R.C.,Accelerated Technologies Center for Gene to 3D Structure (ATCG3D),GPCR Network (GPCR) (deposition date: 2008-05-14, release date: 2008-06-17, Last modification date: 2024-10-30) |
| Primary citation | Hanson, M.A.,Cherezov, V.,Griffith, M.T.,Roth, C.B.,Jaakola, V.P.,Chien, E.Y.,Velasquez, J.,Kuhn, P.,Stevens, R.C. A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure, 16:897-905, 2008 Cited by PubMed Abstract: The role of cholesterol in eukaryotic membrane protein function has been attributed primarily to an influence on membrane fluidity and curvature. We present the 2.8 A resolution crystal structure of a thermally stabilized human beta(2)-adrenergic receptor bound to cholesterol and the partial inverse agonist timolol. The receptors pack as monomers in an antiparallel association with two distinct cholesterol molecules bound per receptor, but not in the packing interface, thereby indicating a structurally relevant cholesterol-binding site between helices I, II, III, and IV. Thermal stability analysis using isothermal denaturation confirms that a cholesterol analog significantly enhances the stability of the receptor. A consensus motif is defined that predicts cholesterol binding for 44% of human class A receptors, suggesting that specific sterol binding is important to the structure and stability of other G protein-coupled receptors, and that this site may provide a target for therapeutic discovery. PubMed: 18547522DOI: 10.1016/j.str.2008.05.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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