The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Cryo-EM structure of the insect olfactory receptor Orco
Open accessAbstract
The olfactory system must recognize and discriminate amongst an enormous variety of chemicals in the environment. To contend with such diversity, insects have evolved a family of odorant-gated ion channels comprised of a highly conserved co-receptor (Orco) and a divergent odorant receptor (OR) that confers chemical specificity. Here, we present the single-particle cryo-electron microscopy structure of an Orco homomer from the parasitic fig wasp Apocrypta bakeri at 3.5 Å resolution, providing structural insight into this receptor family. Orco possesses a novel channel architecture, with four subunits symmetrically arranged around a central pore that diverges into four lateral conduits that open to the cytosol. The Orco tetramer has few inter-subunit interactions within the membrane and is bound together by a small cytoplasmic anchor domain. The minimal sequence conservation among ORs maps largely to the pore and anchor domain, shedding light on how the architecture of this receptor family accommodates its remarkable sequence diversity and facilitates the evolution of odour tuning. A cryo-electron microscopy structure of the insect Orco subunit, which forms ion channels with diverse olfactory receptors, reveals a tetrameric cation channel and sheds light on insect olfaction.
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Metadata
- Authors
- Butterwick, J. A., del Mármol, J., Kim, K. H., Kahlson, M. A., Rogow, J. A., Walz, T., & Ruta, V.
- Venue
- Nature
- Published
- 2018-08
- Volume
- 560
- Issue
- 7719
- Pages
- 447-452
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2885633614
- Cited by
- 462
- References
- 63
- FWCI
- 20.08
- Type
- journal article
- Language
- en
- Open access
- green
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