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Pheromone binding protein

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<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of honey bee complex with pheromone (PDB code [[3bfa]]).' scene=''>
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__TOC__
==Introduction==
==Introduction==
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<StructureSection load='3bfa' size='340' side='right' caption='Pheromone binding protein of ''Apis mellifera'' scene=''>
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'''Pheromone binding proteins''' [http://en.wikipedia.org/wiki/Pheromone_binding_protein (PBP)] are type of Odorant binding proteins [http://en.wikipedia.org/wiki/Odorant-binding_protein (OBP)] - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates<ref>DOI:10.3389/fphys.2014.00320</ref>. The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.
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Pheromone binding proteins [http://en.wikipedia.org/wiki/Pheromone_binding_protein (PBP)] are type of Odorant binding proteins [http://en.wikipedia.org/wiki/Odorant-binding_protein (OBP)] - soluble proteins mediating the early stages of volatiles detection in both insects and vertebrates<ref>DOI:10.3389/fphys.2014.00320</ref>. The volatiles (pheromones and other small hydrophobic molecules) are solubilized by the OBPs and activate the chemoreceptors.
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As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.
As a model protein of this family we will further describe the well investigated Pheromone binding protein of the honey bee, ASP1.
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One of the main components of the QMP <scene name='60/609542/9-oda/3'>9-ODA</scene>, is binding to the protein binding site along with a <scene name='60/609542/Glycerol/2'>glycerol molecule</scene>.The carboxyl end of 9-ODA points towards the solvent, and has no bonds with residues of the protein. The residues in the binding site are <scene name='60/609542/Binding_site/3'>hydrophobic</scene>, and the connection between 9-ODA and ASP1 involve hydrogen bonds.
One of the main components of the QMP <scene name='60/609542/9-oda/3'>9-ODA</scene>, is binding to the protein binding site along with a <scene name='60/609542/Glycerol/2'>glycerol molecule</scene>.The carboxyl end of 9-ODA points towards the solvent, and has no bonds with residues of the protein. The residues in the binding site are <scene name='60/609542/Binding_site/3'>hydrophobic</scene>, and the connection between 9-ODA and ASP1 involve hydrogen bonds.
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==Structure-function relationship==
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</StructureSection>
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==3D structures of pheromone-binding protein==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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* Pheromone binding protein
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**[[2h8v]], [[3bjh]], [[3cab]], [[3cdn]], [[3cz2]] – bPBP residues 26-144 – honey bee<br />
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**[[3d73]], [[3d74]], [[3d75]], [[3d76]], [[3d77]], [[3d78]] - bPBP residues 26-144 (mutant)<br />
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**[[1dqe]], [[2fjy]] – sPBP – silkworm<br />
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**[[1xfr]] – sPBP – NMR<br />
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**[[1gm0]] – sPBP (mutant) – NMR<br />
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**[[1qwv]], [[1two]], [[2jpo]], [[6um9]] – mPBP – moth - NMR<br />
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**[[6vq5]] – mPBP <br />
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**[[7uo6]] – PBP2 – corn borer - NMR<br />
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**[[7vw8]], [[7vw9]] – bwPBP1 - bollworm<br />
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* Pheromone binding protein complex
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**[[3bfa]], [[3bfb]], [[3bfh]], [[3cyz]] – bPBP residues 26-144 + pheromone<br />
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**[[3cz0]], [[3cz1]] - bPBP residues 26-144 + N-butyl benzene sulfonamide<br />
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**[[3fe6]], [[3fe8]], [[3fe9]] - bPBP residues 26-144 + methyldotetracontane<br />
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**[[2p70]] – sPBP + odorant<br />
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**[[2p71]] – sPBP + iodohexadecane<br />
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**[[4inw]], [[4inx]] – PBP + hexadecadienal – ''Amyelois transitella''<br />
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**[[7vwa]] – bwPBP1 + odorant <br />
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}}
== References ==
== References ==
<references/>
<references/>
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[[Category: Topic Page]]

Current revision

Pheromone binding protein of honey bee complex with pheromone (PDB code 3bfa).

Drag the structure with the mouse to rotate

3D structures of pheromone-binding protein

Updated on 23-August-2023

References

  1. ↑ Pelosi P, Iovinella I, Felicioli A, Dani FR. Soluble proteins of chemical communication: an overview across arthropods. Front Physiol. 2014 Aug 27;5:320. doi: 10.3389/fphys.2014.00320. eCollection, 2014. PMID:25221516 doi:http://dx.doi.org/10.3389/fphys.2014.00320
  2. ↑ Winston, M.L., 1987. The Biology of the Honey Bee. Harvard University Press, Cambridge, MA.
  3. ↑ Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C. Structural basis of the honey bee PBP pheromone and pH-induced conformational change. J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083 doi:10.1016/j.jmb.2008.04.048

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