Crystal structure of the beta(2) adrenergic receptor-Gs protein complex

Title
Crystal structure of the beta(2) adrenergic receptor-Gs protein complex
Author
채필석
Keywords
COUPLED RECEPTOR; ADENYLATE-CYCLASE; BETA(2)-ADRENERGIC RECEPTOR; MEDIATED ACTIVATION; LIPIDIC MESOPHASES; MEMBRANE-PROTEINS; ALPHA-SUBUNIT; BINDING; INSIGHTS; CRYSTALLIZATION
Issue Date
2011-09
Publisher
NATURE PUBLISHING GROUP
Citation
NATURE, Vol.477, No.7366 [2011], p549-pU311, 9p.
Abstract
G protein-coupled receptors (GPCRs) are responsible for the majority of cellular responses to hormones and neurotransmitters as well as the senses of sight, olfaction and taste. The paradigm of GPCR signalling is the activation of a heterotrimeric GTP binding protein (G protein) by an agonist-occupied receptor. The beta(2) adrenergic receptor (beta(2)AR) activation of Gs, the stimulatory G protein for adenylyl cyclase, has long been a model system for GPCR signalling. Here we present the crystal structure of the active state ternary complex composed of agonist-occupied monomeric beta(2)AR and nucleotide-free Gs heterotrimer. The principal interactions between the beta(2)AR and Gs involve the amino-and carboxy-terminal a-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the beta(2)AR include a 14 angstrom outward movement at the cytoplasmic end of transmembrane segment 6 (TM6) and an alpha-helical extension of the cytoplasmic end of TM5. The most surprising observation is a major displacement of the alpha-helical domain of G alpha s relative to the Ras-like GTPase domain. This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR.
URI
https://www.nature.com/articles/nature10361http://hdl.handle.net/20.500.11754/36548
ISSN
0028-0836
DOI
10.1038/nature10361
Appears in Collections:
GRADUATE SCHOOL[S](대학원) > BIONANOTECHNOLOGY(바이오나노학과) > Articles
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