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- W1534673860 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." @default.
- W1534673860 created "2016-06-24" @default.
- W1534673860 creator A5031417888 @default.
- W1534673860 creator A5046444163 @default.
- W1534673860 creator A5053521024 @default.
- W1534673860 creator A5058251799 @default.
- W1534673860 creator A5086346963 @default.
- W1534673860 date "2013-01-01" @default.
- W1534673860 modified "2023-09-22" @default.
- W1534673860 title "The Role of Hydrophobic Amino Acids in the Structure and Function of the Rhodopsin Family of G Protein-Coupled Receptors" @default.
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