The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein–bombykol complex
Open accessAbstract
BACKGROUND: Insects use volatile organic molecules to communicate messages with remarkable sensitivity and specificity. In one of the most studied systems, female silkworm moths (Bombyx mori) attract male mates with the pheromone bombykol, a volatile 16-carbon alcohol. In the male moth's antennae, a pheromone-binding protein conveys bombykol to a membrane-bound receptor on a nerve cell. The structure of the pheromone-binding protein, its binding and recognition of bombykol, and its full role in signal transduction are not known. RESULTS: The three-dimensional structure of the B. mori pheromone-binding protein with bound bombykol has been determined by X-ray diffraction at 1.8 A resolution. CONCLUSIONS: The pheromone binding protein of B. mori has six helices, and bombykol binds in a completely enclosed hydrophobic cavity formed by four antiparallel helices. Bombykol is bound in this cavity through numerous hydrophobic interactions, and sequence alignments suggest critical residues for specific pheromone binding.
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Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA
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A look inside odorant-binding proteins in insect chemoreception
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Metadata
- Authors
- Sandler, B. H., Nikonova, L., Leal, W. S., & Clardy, J.
- Venue
- Chemistry & Biology
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 7
- Issue
- 2
- Pages
- 143-151
- ISSN
- 1074-5521 (ISSN-L)
- OpenAlex
- W1974817308
- Cited by
- 481
- References
- 27
- FWCI
- 50.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Sandler, B. H., Nikonova, L., Leal, W. S., & Clardy, J. (2000). Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein–bombykol complex. Chemistry & Biology. https://doi.org/10.1016/s1074-5521(00)00078-8
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