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2R4S

Crystal structure of the human beta2 adrenoceptor

Summary for 2R4S
Entry DOI10.2210/pdb2r4s/pdb
Related2R4R
DescriptorBeta-2 adrenergic receptor, antibody for beta2 adrenoceptor, light chain, antibody for beta2 adrenoceptor, heavy chain (3 entities in total)
Functional Keywordstransmembrane helix, g-protein coupled receptor, glycoprotein, lipoprotein, palmitate, phosphorylation, receptor, transducer, signaling protein
Biological sourceHomo sapiens (human)
More
Cellular locationCell membrane ; Multi- pass membrane protein : P07550
Total number of polymer chains3
Total formula weight86045.80
Authors
Primary citationRasmussen, 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: 17952055
DOI: 10.1038/nature06325
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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