1dqe
From Proteopedia
BOMBYX MORI PHEROMONE BINDING PROTEIN
Structural highlights
FunctionPBP_BOMMO This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBACKGROUND: 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. Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex.,Sandler BH, Nikonova L, Leal WS, Clardy J Chem Biol. 2000 Feb;7(2):143-51. PMID:10662696[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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