Journal article: Journal of Pineal Research

The role of proline residues in the structure and function of human MT2 receptor.

Melatonin functions as an essential regulator of various physiological processes in all vertebrate species. In mammals, two G protein-coupled melatonin receptors (GPCR) mediate some melatonin's actions: MT1 and MT2. Transmembrane domains (TM) of most GPCRs contain a set of highly conserved proline residues that presumably play important structural and functional roles. We investigated the role of proline residues in the structure and function of MT2 receptor: all prolines in TM segments were individually replaced with alanine and/or glycine. Following transient expression in CHO-K1 cells, binding properties of the mutant receptors and their ability to transduce signals were analyzed using I-125-mel- and [S-35]GTP gamma S-binding assays. The impact of the performed mutations on the receptor structure was assessed by molecular dynamic simulations of MT2 receptors embedded in the fully hydrated phospholipid bilayer. Our results indicate that residues P174, P212 and P266 are important for the ligand binding and/or signaling of the human MT2 receptor.
Mazna P, Grycova L, Balik A, Zemkova H, Friedlova E, Obsilova V, Obsil T, Teisinger J: The role of proline residues in the structure and function of human MT2 melatonin receptor. Journal of Pineal Research. 2008; 45(4): 361-372 IF=4,098

Author: obsilovabiomed.cas.cz
 

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