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Polarity conserved positions in transmembrane domains of G‐protein coupled receptors and bacteriorhodopsin
Author(s) -
Zhang Daqun,
Weinstein Harel
Publication year - 1994
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 - 10.1016/0014-5793(94)80274-2
Subject(s) - bacteriorhodopsin , g protein coupled receptor , transmembrane domain , transmembrane protein , polarity (international relations) , helix (gastropod) , membrane protein , biology , conserved sequence , biophysics , chemistry , crystallography , receptor , peptide sequence , biochemistry , membrane , gene , ecology , snail , cell
The polarity of residues at certain positions in the transmembrane domains of G‐protein coupled receptors (GPCR) is found to be conserved, and to indicate the pattern of specific helix‐helix packing of the helices. A concept of polarity conserved positions (PCP) is proposed to describe this conserved property, and is applied to obtain insight into the structural features of the transmembrane proteins. The common pattern of PCPs for GPCRs indicates that they share a similar packing arrangement of their transmembrane helix bundles. For proteins in the bacteriorhodopsin family the PCP pattern suggests a common packing arrangement that differs from that of GPCRs, in agreement with experimental data. This difference in the packing arrangement underscores the shortcomings of a BR template for the construction of molecular models of GPCRs.