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| {{STRUCTURE_1dqe| PDB=1dqe | SCENE= }} | | {{STRUCTURE_1dqe| PDB=1dqe | SCENE= }} |
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| '''BOMBYX MORI PHEROMONE BINDING PROTEIN'''
| | ===BOMBYX MORI PHEROMONE BINDING PROTEIN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10662696}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10662696 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10662696}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sandler, B H.]] | | [[Category: Sandler, B H.]] |
| [[Category: Helical bundle]] | | [[Category: Helical bundle]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:09:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:27:49 2008'' |
