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

Thomas A. Hopf, Satoshi Morinaga, Sayoko Ihara, Kazushige Touhara, Debora S. Marks and Richard Benton ()
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Thomas A. Hopf: Harvard Medical School
Satoshi Morinaga: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Sayoko Ihara: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Kazushige Touhara: Graduate School of Agricultural and Life Sciences, The University of Tokyo
Debora S. Marks: Harvard Medical School
Richard Benton: Center for Integrative Genomics, Faculty of Biology and Medicine, University of Lausanne

Nature Communications, 2015, vol. 6, issue 1, 1-7

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7077

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