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1dqe

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[[Image:1dqe.gif|left|200px]]
 
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{{Structure
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==BOMBYX MORI PHEROMONE BINDING PROTEIN==
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|PDB= 1dqe |SIZE=350|CAPTION= <scene name='initialview01'>1dqe</scene>, resolution 1.8&Aring;
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<StructureSection load='1dqe' size='340' side='right'caption='[[1dqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BOM:HEXADECA-10,12-DIEN-1-OL'>BOM</scene>
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<table><tr><td colspan='2'>[[1dqe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DQE FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOM:HEXADECA-10,12-DIEN-1-OL'>BOM</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqe OCA], [https://pdbe.org/1dqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dqe RCSB], [https://www.ebi.ac.uk/pdbsum/1dqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqe ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqe OCA], [http://www.ebi.ac.uk/pdbsum/1dqe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dqe RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PBP_BOMMO PBP_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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqe_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dqe ConSurf].
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<div style="clear:both"></div>
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'''BOMBYX MORI PHEROMONE BINDING PROTEIN'''
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==See Also==
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*[[Pheromone binding protein|Pheromone binding protein]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1DQE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQE OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10662696 10662696]
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[[Category: Bombyx mori]]
[[Category: Bombyx mori]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Clardy, J.]]
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[[Category: Clardy J]]
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[[Category: Leal, W S.]]
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[[Category: Leal WS]]
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[[Category: Nikonova, L.]]
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[[Category: Nikonova L]]
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[[Category: Sandler, B H.]]
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[[Category: Sandler BH]]
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[[Category: helical bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:46:38 2008''
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Current revision

BOMBYX MORI PHEROMONE BINDING PROTEIN

PDB ID 1dqe

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