2r4s
Crystal structure of the human beta2 adrenoceptor
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OverviewOverview
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 beta(2) adrenoceptor (beta(2)AR), 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 beta(2)AR transmembrane segments, and the connecting loops are well resolved, whereas the extracellular, regions of the beta(2)AR are not seen. The beta(2)AR 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 beta(2)AR, and contribute to, the challenges in obtaining diffraction-quality crystals of non-rhodopsin, GPCRs.
About this StructureAbout this Structure
2R4S is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human beta(2) adrenergic G-protein-coupled receptor., Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK, Nature. 2007 Oct 21;. PMID:17952055
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