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

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

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Title: Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors
Author: Hopf, Thomas A.; Morinaga, Satoshi; Ihara, Sayoko; Touhara, Kazushige; Marks, Debora S.; Benton, Richard

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Citation: Hopf, Thomas A., Satoshi Morinaga, Sayoko Ihara, Kazushige Touhara, Debora S. Marks, and Richard Benton. 2015. “Amino acid coevolution reveals three-dimensional structure and functional domains of insect odorant receptors.” Nature communications 6 (1): 6077. doi:10.1038/ncomms7077. http://dx.doi.org/10.1038/ncomms7077.
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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.
Published Version: doi:10.1038/ncomms7077
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4364406/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:17820906
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