Identifying G protein-coupled receptor dimers from crystal packings

被引:14
作者
Stenkamp, Ronald E. [1 ,2 ]
机构
[1] Univ Washington, Biomol Struct Ctr, Dept Biol Struct, Box 357420, Seattle, WA 98195 USA
[2] Univ Washington, Biomol Struct Ctr, Dept Biochem, Box 357420, Seattle, WA 98195 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2018年 / 74卷
关键词
G-protein-coupled receptors; GPCRs; dimers; crystal-packing interactions; ENDOTHELIN ETB-RECEPTOR; STRUCTURAL BASIS; OPIOID RECEPTOR; FUNCTIONAL SELECTIVITY; CHEMOKINE RECOGNITION; LIGAND RECOGNITION; RHODOPSIN; COMPLEX; GPCR; ACTIVATION;
D O I
10.1107/S2059798318008136
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Dimers of G protein-coupled receptors (GPCRs) are believed to be important for signaling with their associated G proteins. Low-resolution electron microscopy has shown rhodopsin dimers in native retinal membranes, and CXCR4 dimers have been found in several different crystal structures. Evidence for dimers of other GPCRs is more indirect. An alternative to computational modeling studies is to search for parallel dimers in the packing environments of the reported crystal structures of GPCRs. Two major structural types of GPCR dimers exist (as predicted by others), but there is considerable structural variation within each cluster. The different structural variants described here might reflect different functional properties and should provide a range of model structures for computational and experimental examination.
引用
收藏
页码:655 / 670
页数:16
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