2r4s

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{{STRUCTURE_2r4s| PDB=2r4s | SCENE= }}
{{STRUCTURE_2r4s| PDB=2r4s | SCENE= }}
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'''Crystal structure of the human beta2 adrenoceptor'''
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===Crystal structure of the human beta2 adrenoceptor===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17952055}}
==About this Structure==
==About this Structure==
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[[Category: Transducer]]
[[Category: Transducer]]
[[Category: Transmembrane helix]]
[[Category: Transmembrane helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:14:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 9 10:08:09 2008''

Revision as of 07:08, 9 July 2008

Image:2r4s.png

Template:STRUCTURE 2r4s

Crystal structure of the human beta2 adrenoceptor

Template:ABSTRACT PUBMED 17952055

About this Structure

2R4S is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human beta2 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 Nov 15;450(7168):383-7. Epub 2007 Oct 21. PMID:17952055

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