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

Methods Enzymol. 2013;520:99-115. doi: 10.1016/B978-0-12-391861-1.00005-8.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Animals
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Receptors, G-Protein-Coupled / chemistry*
  • Receptors, G-Protein-Coupled / metabolism*
  • Rhodopsin / chemistry*
  • Rhodopsin / metabolism*
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Receptors, G-Protein-Coupled
  • Rhodopsin