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

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 O

SUBMITTER: Hopf TA 

PROVIDER: S-EPMC4364406 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature