Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.

Details

Ressource 1Download: BIB_0D6E80DE4092.P001.pdf (1696.21 [Ko])
State: Public
Version: author
Serval ID
serval:BIB_0D6E80DE4092
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.
Journal
Nature Communications
Author(s)
Hopf T.A., Morinaga S., Ihara S., Touhara K., Marks D.S., Benton R.
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Publication state
Published
Issued date
2015
Peer-reviewed
Oui
Volume
6
Number
6077
Pages
6077
Language
english
Abstract
Insect odorant receptors (ORs) comprise an enormous protein family that translates environmental chemical signals into neuronal electrical activity. These heptahelical receptors are proposed to function as ligand-gated ion channels and/or to act metabotropically as G protein-coupled receptors (GPCRs). Resolving their signalling mechanism has been hampered by the lack of tertiary structural information and primary sequence similarity to other proteins. We use amino acid evolutionary covariation across these ORs to define restraints on structural proximity of residue pairs, which permit de novo generation of three-dimensional models. The validity of our analysis is supported by the location of functionally important residues in highly constrained regions of the protein. Importantly, insect OR models exhibit a distinct transmembrane domain packing arrangement to that of canonical GPCRs, establishing the structural unrelatedness of these receptor families. The evolutionary couplings and models predict odour binding and ion conduction domains, and provide a template for rationale structure-activity dissection.
Pubmed
Web of science
Open Access
Yes
Create date
09/01/2015 10:26
Last modification date
20/08/2019 12:34
Usage data