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Crystal structure of the β2 adrenergic receptor–Gs protein complex

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-occupi... Full description

Journal Title: Nature 2011, Vol.477(7366), p.549
Main Author: Søren G. F. Rasmussen
Other Authors: Brian T. Devree , Yaozhong Zou , Andrew C. Kruse , Ka Young Chung , Tong Sun Kobilka , Foon Sun Thian , Pil Seok Chae , Els Pardon , Diane Calinski , Jesper M. Mathiesen , Syed T. A. Shah , Joseph A. Lyons , Martin Caffrey , Samuel H. Gellman , Jan Steyaert , Georgios Skiniotis , William I. Weis , Roger K. Sunahara , Brian K. Kobilka
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ID: ISSN: 0028-0836 ; E-ISSN: 1476-4687 ; DOI: 10.1038/nature10361
Link: http://dx.doi.org/10.1038/nature10361
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recordid: nature_a10.1038/nature10361
title: Crystal structure of the β2 adrenergic receptor–Gs protein complex
format: Article
creator:
  • Søren G. F. Rasmussen
  • Brian T. Devree
  • Yaozhong Zou
  • Andrew C. Kruse
  • Ka Young Chung
  • Tong Sun Kobilka
  • Foon Sun Thian
  • Pil Seok Chae
  • Els Pardon
  • Diane Calinski
  • Jesper M. Mathiesen
  • Syed T. A. Shah
  • Joseph A. Lyons
  • Martin Caffrey
  • Samuel H. Gellman
  • Jan Steyaert
  • Georgios Skiniotis
  • William I. Weis
  • Roger K. Sunahara
  • Brian K. Kobilka
subjects:
  • G Proteins -- Research
  • G Proteins -- Physiological Aspects
  • Adrenergic Receptors -- Structure
  • Adrenergic Receptors -- Research
  • Gtpases -- Physiological Aspects
  • Gtpases -- Research
ispartof: Nature, 2011, Vol.477(7366), p.549
description: 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].sub.2] adrenergic receptor ([[beta].sub.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].sub.2]AR and nucleotide-free Gs heterotrimer. The principal interactions between the [[beta].sub.2]AR and Gs involve the amino- and carboxy-terminal [alpha]-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the [[beta].sub.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.
language:
source:
identifier: ISSN: 0028-0836 ; E-ISSN: 1476-4687 ; DOI: 10.1038/nature10361
fulltext: fulltext
issn:
  • 0028-0836
  • 00280836
  • 1476-4687
  • 14764687
url: Link


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titleCrystal structure of the β2 adrenergic receptor–Gs protein complex
creatorSøren G. F. Rasmussen ; Brian T. Devree ; Yaozhong Zou ; Andrew C. Kruse ; Ka Young Chung ; Tong Sun Kobilka ; Foon Sun Thian ; Pil Seok Chae ; Els Pardon ; Diane Calinski ; Jesper M. Mathiesen ; Syed T. A. Shah ; Joseph A. Lyons ; Martin Caffrey ; Samuel H. Gellman ; Jan Steyaert ; Georgios Skiniotis ; William I. Weis ; Roger K. Sunahara ; Brian K. Kobilka
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subjectG Proteins -- Research ; G Proteins -- Physiological Aspects ; Adrenergic Receptors -- Structure ; Adrenergic Receptors -- Research ; Gtpases -- Physiological Aspects ; Gtpases -- Research;
descriptionG 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].sub.2] adrenergic receptor ([[beta].sub.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].sub.2]AR and nucleotide-free Gs heterotrimer. The principal interactions between the [[beta].sub.2]AR and Gs involve the amino- and carboxy-terminal [alpha]-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the [[beta].sub.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.
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