1ls8

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[[Image:1ls8.png|left|200px]]
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==NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH==
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<StructureSection load='1ls8' size='340' side='right' caption='[[1ls8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ls8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LS8 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ls8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ls8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ls8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ls8 PDBsum]</span></td></tr>
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<table>
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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/ls/1ls8_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/chain_selection.php?pdb_ID=2ata 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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The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide bridges 19-54, 50-108, and 97-117. This polypeptide fold encloses a large hydrophobic cavity, with a sufficient volume to accommodate the natural ligand bombykol. The polypeptide folds in free BmPBP(B) and in crystals of a BmPBP-bombykol complex are nearly identical, indicating that the B-form of BmPBP in solution represents the active conformation for ligand binding.
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{{STRUCTURE_1ls8| PDB=1ls8 | SCENE= }}
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NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH.,Lee D, Damberger FF, Peng G, Horst R, Guntert P, Nikonova L, Leal WS, Wuthrich K FEBS Lett. 2002 Nov 6;531(2):314-8. PMID:12417333<ref>PMID:12417333</ref>
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===NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH===
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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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{{ABSTRACT_PUBMED_12417333}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1ls8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS8 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012417333</ref><references group="xtra"/>
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[[Category: Bombyx mori]]
[[Category: Bombyx mori]]
[[Category: Damberger, F.]]
[[Category: Damberger, F.]]

Revision as of 15:21, 28 September 2014

NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH

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