4n1j

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'''Unreleased structure'''
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==Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions==
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<StructureSection load='4n1j' size='340' side='right' caption='[[4n1j]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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The entry 4n1j is ON HOLD until Paper Publication
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4n1j]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N1J FirstGlance]. <br>
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Authors: Eibl, C., Hessenberger, M., Wenger, J., Brandstetter, H.
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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Description: Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1k|4n1k]], [[4n1l|4n1l]]</td></tr>
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<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=4n1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n1j RCSB], [http://www.ebi.ac.uk/pdbsum/4n1j PDBsum]</span></td></tr>
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<table>
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__TOC__
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</StructureSection>
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[[Category: Brandstetter, H.]]
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[[Category: Eibl, C.]]
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[[Category: Hessenberger, M.]]
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[[Category: Wenger, J.]]
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[[Category: Death domain fold]]
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[[Category: Innate immunity]]
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[[Category: Nod-like receptor]]
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[[Category: Protein binding]]
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[[Category: Pyrin domain]]
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[[Category: Signaling protein]]
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[[Category: Spermatogenesis]]

Revision as of 10:28, 16 July 2014

Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions

4n1j, resolution 2.60Å

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