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Default Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

Related Articles Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein-coupled receptors.

FEBS Lett. 2019 Apr 05;:

Authors: Hu W, Wang H, Hou Y, Hao Y, Liu D

Abstract
Large membrane proteins such as G Protein-Coupled Receptors (GPCRs) are difficult for NMR study due to severe signal overlaps and unfavorable relaxation properties. We used a trimethylsilyl (TMS) group as a reporter group for 1 H NMR study of conformational changes in proteins, utilizing high-intensity 1 H NMR signals near 0 ppm. The ?2 -Adrenergic Receptor (?2 AR) was labeled with TMS groups at two cysteines located at the cytoplasmic ends of helices VI and VII. Binding of various ligands led to changes in 1 H NMR signals, which manifested that helix VI is sensitive to G protein-specific activation, whereas helix VII is sensitive to ?-arrestin-specific activation. Thus, the TMS group is a useful reporter group in NMR for studying conformational changes in membrane proteins such as GPCRs. This article is protected by copyright. All rights reserved.


PMID: 30953343 [PubMed - as supplied by publisher]



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