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Analysis of secondary structures of odorant receptors
Author(s) -
Nguy May,
Qiu Rongde,
Feng YingHong
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.722.3
Subject(s) - rhodopsin , g protein coupled receptor , subfamily , transmembrane domain , rhodopsin like receptors , helix (gastropod) , biology , conserved sequence , receptor , ligand (biochemistry) , structural motif , chemistry , biochemistry , stereochemistry , peptide sequence , gene , ecology , retinal , glutamate receptor , metabotropic receptor , snail
The structure‐function relationship of rhodopsin family GPCRs is well studied whereas little is known about the family of G protein‐coupled odorant receptors (ORs). Here the amino acid sequences and the functional domains of 385 human ORs were analyzed using AlignX, transmembrane (TM) helix prediction, and helix wheel projection. Most importantly, the critical residues, motifs and domains of ORs were examined by comparison with the corresponding ones of the rhodopsin family, especially the bioamine subfamily GPCRs that bind ligands with small size. Our result shows that as many as 59 residues in the TM domains and 33 residues in the non‐TM domains are conserved in >90% of ORs, an increase of 36.1% over 36 residues in the TM domains of the rhodopsin family GPCRs. Interestingly, the distributions of the highly conserved residues are largely distinct between the two family GPCRs, especially, in TM2, TM3, TM4, TM6 and TM7. The TM3 of ORs bearing highly conserved DRY motif for activation of Gα proteins was found to be one residue longer than that of the rhodopsin family GPCRs. These results suggest that ORs may have unique, but rather conserved global conformation and utilize structural mechanisms distinct from GPCRs of the rhodopsin family for ligand binding and activation. Supported by ASPET SURF award to MN and NIH grant (HL065492) to YHF