Sandbox bcce16
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==Bombyx mori pheromone binding protein (PBP)== | ==Bombyx mori pheromone binding protein (PBP)== | ||
| - | <StructureSection load='1dqe' size='340' side='right' caption='Caption for this structure' scene='59/596450/Bmori_pbp/ | + | <StructureSection load='1dqe' size='340' side='right' caption='Caption for this structure' scene='59/596450/Bmori_pbp/3'> |
The antenna of the male B. mori silkworm moth is exquisitely sensitive to the female sex pheromone bombykol; as little as 3,000 molecules of bombykol per mL of air can evoke a behavioral response. This sensitivity requires the use of the pheromone binding protein (PBP) to carry the highly hydrophobic pheromone through the aqueous environment of the sensillary lymph to odorant receptors on the olfactory neuron. | The antenna of the male B. mori silkworm moth is exquisitely sensitive to the female sex pheromone bombykol; as little as 3,000 molecules of bombykol per mL of air can evoke a behavioral response. This sensitivity requires the use of the pheromone binding protein (PBP) to carry the highly hydrophobic pheromone through the aqueous environment of the sensillary lymph to odorant receptors on the olfactory neuron. | ||
== Function == | == Function == | ||
| - | The B. mori PBP contains an interior, hydrophobic pocket into which the pheromone ligand binds. A conserved serine forms hydrogen | + | The B. mori PBP contains an interior, hydrophobic pocket into which the pheromone ligand binds. A conserved residue, |
| + | <scene name='59/596450/Bmori_pbp_ser56/1'>serine 56,</scene> forms a hydrogen bond with the hydroxyl functional group of the pheromone; this is mutated to alanine in lepidopteran species which use acetyl esters as pheromones. Some species with multiple pheromone components possess multiple PBP isoforms, suggesting a role in odorant discrimination as well. | ||
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| + | Once the PBP reaches the odorant receptor at the neuronal membrane, it ejects the bound pheromone molecule via a pH-dependent conformational change. In the binding-competent high-pH form, the C-terminal residues 131-142 form a <scene name='59/596450/Bmori_pbp_open/1'>disordered surface loop</scene>. But in the non-binding low-pH form, these residues form an <scene name='59/596450/Bmori_pbp_closed/4'>alpha helix</scene> that fills the ligand binding site. | ||
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| - | <scene name='59/596450/Bmori_pbp/1'>TextToBeDisplayed</scene> | ||
| - | == Structural highlights == | ||
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
| + | <ref>PMID:10662696</ref> | ||
| + | <ref>PMID:11724947</ref> | ||
<references/> | <references/> | ||
Current revision
Bombyx mori pheromone binding protein (PBP)
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References
- ↑ Sandler BH, Nikonova L, Leal WS, Clardy J. Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex. Chem Biol. 2000 Feb;7(2):143-51. PMID:10662696
- ↑ Horst R, Damberger F, Luginbuhl P, Guntert P, Peng G, Nikonova L, Leal WS, Wuthrich K. NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14374-9. Epub 2001 Nov 27. PMID:11724947 doi:10.1073/pnas.251532998
