@inbook{11fbab773a504546a374f7577625d460,
title = "The role of hydrophobic amino acids in the structure and function of the rhodopsin family of G protein-coupled receptors",
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. {\textcopyright} 2013 Elsevier Inc.",
keywords = "Activation, G protein, Hydrophobic residues, Keywords, Oligomerization, Structure and function, coupled receptors",
author = "Gianluigi Caltabiano and Angel Gonzalez and Arnau Cordom{\'i} and Mercedes Campillo and Leonardo Pardo",
year = "2013",
month = jan,
day = "1",
doi = "10.1016/B978-0-12-391861-1.00005-8",
language = "English",
isbn = "0076-6879",
volume = "520",
series = "Methods in Enzymology",
publisher = "Elsevier Inc.",
pages = "99--115",
booktitle = "G Protein Coupled Receptor: Structure",
address = "United States",
edition = "1",
}