Uncovering the triggers for GPCR activation using solid-state NMR spectroscopy

Naoki Kimata, Philip J. Reeves, Steven O. Smith*

*この研究の対応する著者

研究成果: Article査読

10 被引用数 (Scopus)

抄録

Abstract G protein-coupled receptors (GPCRs) span cell membranes with seven transmembrane helices and respond to a diverse array of extracellular signals. Crystal structures of GPCRs have provided key insights into the architecture of these receptors and the role of conserved residues. However, the question of how ligand binding induces the conformational changes that are essential for activation remains largely unanswered. Since the extracellular sequences and structures of GPCRs are not conserved between receptor subfamilies, it is likely that the initial molecular triggers for activation vary depending on the specific type of ligand and receptor. In this article, we describe NMR studies on the rhodopsin subfamily of GPCRs and propose a mechanism for how retinal isomerization switches the receptor to the active conformation. These results suggest a general approach for determining the triggers for activation in other GPCR subfamilies using NMR spectroscopy.

本文言語English
論文番号5577
ページ(範囲)111-118
ページ数8
ジャーナルJournal of Magnetic Resonance
253
DOI
出版ステータスPublished - 2015 4月
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 核物理学および高エネルギー物理学
  • 凝縮系物理学

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