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4n1j

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==Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions==
==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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<StructureSection load='4n1j' size='340' side='right'caption='[[4n1j]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== 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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<table><tr><td colspan='2'>[[4n1j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4N1J FirstGlance]. <br>
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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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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1j OCA], [https://pdbe.org/4n1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1j RCSB], [https://www.ebi.ac.uk/pdbsum/4n1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1j ProSAT]</span></td></tr>
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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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</table>
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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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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/NAL14_HUMAN NAL14_HUMAN] May be involved in inflammation and spermatogenesis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The cytosolic tripartite NLR receptors serve as important signalling platforms in innate immunity. While the C-terminal domains act as sensor and activation modules, the N-terminal death-like domain, e.g. the CARD or pyrin domain, is thought to recruit downstream effector molecules by homotypic interactions. Such homotypic complexes have been determined for all members of the death-domain superfamily except for pyrin domains. Here, crystal structures of human NLRP14 pyrin-domain variants are reported. The wild-type protein as well as the clinical D86V mutant reveal an unexpected rearrangement of the C-terminal helix alpha6, resulting in an extended alpha5/6 stem-helix. This reordering mediates a novel symmetric pyrin-domain dimerization mode. The conformational switching is controlled by a charge-relay system with a drastic impact on protein stability. How the identified charge relay allows classification of NLRP receptors with respect to distinct recruitment mechanisms is discussed.
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Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.,Eibl C, Hessenberger M, Wenger J, Brandstetter H Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):2007-18. doi:, 10.1107/S1399004714010311. Epub 2014 Jun 29. PMID:25004977<ref>PMID:25004977</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 4n1j" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Pyrin domain|Pyrin domain]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brandstetter, H.]]
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[[Category: Homo sapiens]]
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[[Category: Eibl, C.]]
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[[Category: Large Structures]]
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[[Category: Hessenberger, M.]]
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[[Category: Brandstetter H]]
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[[Category: Wenger, J.]]
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[[Category: Eibl C]]
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[[Category: Death domain fold]]
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[[Category: Hessenberger M]]
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[[Category: Innate immunity]]
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[[Category: Wenger J]]
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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]]
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Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions

PDB ID 4n1j

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