2R4S
Crystal structure of the human beta2 adrenoceptor
Summary for 2R4S
| Entry DOI | 10.2210/pdb2r4s/pdb |
| Related | 2R4R |
| Descriptor | Beta-2 adrenergic receptor, antibody for beta2 adrenoceptor, light chain, antibody for beta2 adrenoceptor, heavy chain (3 entities in total) |
| Functional Keywords | transmembrane helix, g-protein coupled receptor, glycoprotein, lipoprotein, palmitate, phosphorylation, receptor, transducer, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane ; Multi- pass membrane protein : P07550 |
| Total number of polymer chains | 3 |
| Total formula weight | 86045.80 |
| Authors | Rasmussen, S.G.F.,Choi, H.J.,Rosenbaum, D.M.,Kobilka, T.S.,Thian, F.S.,Edwards, P.C.,Burghammer, M.,Ratnala, V.R.,Sanishvili, R.,Fischetti, R.F.,Schertler, G.F.,Weis, W.I.,Kobilka, B.K. (deposition date: 2007-08-31, release date: 2007-11-06, Last modification date: 2024-10-16) |
| Primary citation | Rasmussen, S.G.F.,Choi, H.J.,Rosenbaum, D.M.,Kobilka, T.S.,Thian, F.S.,Edwards, P.C.,Burghammer, M.,Ratnala, V.R.,Sanishvili, R.,Fischetti, R.F.,Schertler, G.F.,Weis, W.I.,Kobilka, B.K. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature, 450:383-387, 2007 Cited by PubMed Abstract: Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs. PubMed: 17952055DOI: 10.1038/nature06325 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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