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Ligand binding to the human MT2 melatonin receptor: the role of residues in transmembrane domains 3, 6, and 7.

Abstract：

:To better understand the mechanism of interactions between G-protein-coupled melatonin receptors and their ligands, our previously reported homology model of human MT2 receptor with docked 2-iodomelatonin was further refined and used to select residues within TM3, TM6, and TM7 potentially important for receptor-ligand interactions. Selected residues were mutated and radioligand-binding assay was used to test the binding affinities of hMT2 receptors transiently expressed in HEK293 cells. Our data demonstrate that residues N268 and A275 in TM6 as well as residues V291 and L295 in TM7 are essential for 2-iodomelatonin binding to the hMT2 receptor, while TM3 residues M120, G121, V124, and I125 may participate in binding of other receptor agonists and/or antagonists. Presented data also hint at possible specific interaction between the side-chain of Y188 in second extracellular loop and N-acetyl group of 2-iodomelatonin.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mazna P,Berka K,Jelinkova I,Balik A,Svoboda P,Obsilova V,Obsil T,Teisinger J

doi

10.1016/j.bbrc.2005.05.017

subject

Has Abstract

pub_date

2005-07-08 00:00:00

pages

726-34

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)00968-X

journal_volume

332

pub_type

杂志文章

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