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

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Etat: Serval
Version: de l'auteur
ID Serval
serval:BIB_0D6E80DE4092
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.
Périodique
Nature Communications
Auteur(s)
Hopf T.A., Morinaga S., Ihara S., Touhara K., Marks D.S., Benton R.
ISSN
2041-1723 (Electronic)
ISSN-L
2041-1723
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
6
Numéro
6077
Pages
6077
Langue
anglais
Résumé
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
Création de la notice
09/01/2015 11:26
Dernière modification de la notice
03/03/2018 13:40
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