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The arrangement of the transmembrane helices in the secretin receptor family of G‐protein‐coupled receptors
Author(s) -
Donnelly Dan
Publication year - 1997
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 - 10.1016/s0014-5793(97)00546-2
Subject(s) - rhodopsin , helix bundle , transmembrane domain , helix (gastropod) , lipid bilayer , receptor , transmembrane protein , bilayer , g protein coupled receptor , sequence (biology) , secretin , crystallography , peptide sequence , biophysics , chemistry , biology , protein structure , biochemistry , membrane , gene , ecology , retinal , secretion , snail
The members of the secretin receptor family of G‐protein‐coupled receptors share no significant sequence similarity to the more familiar rhodopsin‐like family. However, multiple sequence alignment analysis reveals seven hydrophobic regions with significant α‐helical periodicity. Residues that are likely to be buried on the interior of the helical bundle and others that are likely to contact the lipid bilayer are identified. A predicted arrangement of the helical bundle is described in which, by comparison with the arrangement in the rhodopsin family, helices 2 and 7 are more buried within the bundle while helix 3 is more exposed to the lipid bilayer.