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| {{STRUCTURE_2fjy| PDB=2fjy | SCENE= }} | | {{STRUCTURE_2fjy| PDB=2fjy | SCENE= }} |
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| '''Crystal Structure of B-form Bombyx mori Pheromone Binding Protein'''
| | ===Crystal Structure of B-form Bombyx mori Pheromone Binding Protein=== |
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| ==Overview==
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| The transport of hydrophobic insect pheromones through the aqueous medium surrounding their receptors is assisted by pheromone-binding proteins (PBPs). The protein from the silkworm moth Bombyx mori, BmorPBP, exhibits a pH-dependent conformational change postulated to trigger the release of the pheromone bombykol to its receptor. At low pH, an alpha-helix occupies the same binding pocket that houses the pheromone in the BmorPBP-bombykol complex at high pH. We have determined the crystal structure of apo BmorPBP at a resolution of 2.3 angstroms and pH 7.5, which has surprisingly a structure similar to the A-form. These data suggest that BmorPBP undergoes a ligand-dependent conformational change in addition to the previously described pH-dependent conformational change. Analysis of the alpha-helix occupying the binding pocket reveals an amphipathic helix with three acidic residues along one face that are conserved among lepidopteran PBPs and may be involved in a conformational transition of BmorPBP at the receptor membrane. | | The line below this paragraph, {{ABSTRACT_PUBMED_16111659}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16111659 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16111659}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Leal, W S.]] | | [[Category: Leal, W S.]] |
| [[Category: Alpha helical]] | | [[Category: Alpha helical]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:59:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:36:15 2008'' |
