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.
authors: Laboratori de Medicina Computacional, Unitat de Bioestadística, Facultat de Medicina, Universitat Autònoma de Barcelona, Barcelona, Spain.
authors: Gianluigi
authors: G
authors: Caltabiano
authors: Angel
authors: A
authors: Gonzalez
authors: Arnau
authors: A
authors: Cordomí
authors: Mercedes
authors: M
authors: Campillo
authors: Leonardo
authors: L
authors: Pardo
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D000818:Animals; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D000596:Amino Acids; D043562:Receptors, G-Protein-Coupled; D012243:Rhodopsin