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Trimethylsilyl reporter groups for NMR studies of conformational changes in G protein‐coupled receptors
Author(s) -
Hu Wanhui,
Wang Huixia,
Hou Yaguang,
Hao Yimei,
Liu Dongsheng
Publication year - 2019
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13382
Subject(s) - chemistry , g protein coupled receptor , helix (gastropod) , receptor , trimethylsilyl , stereochemistry , g protein , biophysics , biochemistry , biology , organic chemistry , ecology , snail
Large membrane proteins such as G protein‐coupled receptors ( GPCR s) 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 p.p.m. The β 2 ‐adrenergic receptor 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 β‐arrestin‐specific activation. Thus, the TMS group is a useful reporter group in NMR for studying conformational changes in membrane proteins such as GPCR s.