| Title: | Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex |
| Author(s): | Sandler BH; Nikonova L; Leal WS; Clardy J; |
| Address: | "Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA" |
| DOI: | 10.1016/s1074-5521(00)00078-8 |
| ISSN/ISBN: | 1074-5521 (Print) 1074-5521 (Linking) |
| Abstract: | "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" |
| Keywords: | "Amino Acid Sequence Animals Binding Sites Bombyx/*chemistry/physiology Crystallization Fatty Alcohols/*chemistry/metabolism Female Hydrogen-Ion Concentration Male Models, Molecular Molecular Sequence Data Pheromones/metabolism Protein Structure, Secondary;" |
| Notes: | "MedlineSandler, B H Nikonova, L Leal, W S Clardy, J eng CA24487/CA/NCI NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 2000/02/09 Chem Biol. 2000 Feb; 7(2):143-51. doi: 10.1016/s1074-5521(00)00078-8" |
