The role of hydrophobic amino acids in the structure and function of the rhodopsin family of G protein-coupled receptors

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Abstract

Recent advances in crystallization methods have permitted to resolve the molecular structure of several members of the rhodopsin family of G protein-coupled receptors (GPCRs). Comparison among these structures revealed a number of conserved polar and charged residues implicated in the receptor transduction pathways. These residues function as micro-switches in the process of receptor activation and has been the object of study of many research groups. However, hydrophobic forces, usually underappreciated, also play a major role in GPCR function. Conserved hydrophobic residues contribute significantly to receptor activation, G protein coupling, and oligomerization processes. This review focuses on the impact of the hydrophobic amino acids observed in the structure of class A GPCRs necessary for their function. This information represents a fundamental piece to complete a holistic view of the GPCR signal transduction machinery. © 2013 Elsevier Inc.
Original languageEnglish
Title of host publicationG Protein Coupled Receptor: Structure
Place of Publication(DE)
Pages99-115
Number of pages16
Volume520
Edition1
ISBN (Electronic)1557-7988
DOIs
Publication statusPublished - 1 Jan 2013

Publication series

NameMethods in Enzymology

Keywords

  • Activation
  • G protein
  • Hydrophobic residues
  • Keywords
  • Oligomerization
  • Structure and function
  • coupled receptors

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