1dqe

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{{Seed}}
 
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[[Image:1dqe.png|left|200px]]
 
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==BOMBYX MORI PHEROMONE BINDING PROTEIN==
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The line below this paragraph, containing "STRUCTURE_1dqe", creates the "Structure Box" on the page.
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<StructureSection load='1dqe' size='340' side='right'caption='[[1dqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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<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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{{STRUCTURE_1dqe| PDB=1dqe | SCENE= }}
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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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</table>
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== Function ==
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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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===BOMBYX MORI PHEROMONE BINDING PROTEIN===
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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:10662696<ref>PMID:10662696</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1dqe" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10662696}}, adds the Publication Abstract to the page
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*[[Pheromone binding protein|Pheromone binding protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10662696 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10662696}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1DQE is a 2 chains structure of sequences 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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<ref group="xtra">PMID:10662696</ref><references group="xtra"/>
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[[Category: Bombyx mori]]
[[Category: Bombyx mori]]
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[[Category: Clardy, J.]]
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[[Category: Large Structures]]
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[[Category: Leal, W S.]]
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[[Category: Clardy J]]
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[[Category: Nikonova, L.]]
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[[Category: Leal WS]]
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[[Category: Sandler, B H.]]
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[[Category: Nikonova L]]
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[[Category: Helical bundle]]
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[[Category: Sandler BH]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:30:04 2009''
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Current revision

BOMBYX MORI PHEROMONE BINDING PROTEIN

PDB ID 1dqe

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