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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==
<StructureSection load='4n1l' size='340' side='right' caption='[[4n1l]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='4n1l' size='340' side='right'caption='[[4n1l]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4n1l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N1L FirstGlance]. <br>
<table><tr><td colspan='2'>[[4n1l]] is a 1 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=4N1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N1L FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1j|4n1j]], [[4n1k|4n1k]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.986&#8491;</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=4n1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n1l RCSB], [http://www.ebi.ac.uk/pdbsum/4n1l PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1l OCA], [https://pdbe.org/4n1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1l RCSB], [https://www.ebi.ac.uk/pdbsum/4n1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1l ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NAL14_HUMAN NAL14_HUMAN] May be involved in inflammation and spermatogenesis.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4n1l" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Pyrin domain|Pyrin domain]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Brandstetter, H.]]
[[Category: Homo sapiens]]
[[Category: Eibl, C.]]
[[Category: Large Structures]]
[[Category: Hessenberger, M.]]
[[Category: Brandstetter H]]
[[Category: Wenger, J.]]
[[Category: Eibl C]]
[[Category: Death domain fold]]
[[Category: Hessenberger M]]
[[Category: Innate immunity]]
[[Category: Wenger J]]
[[Category: Nod-like receptor]]
[[Category: Protein binding]]
[[Category: Pyrin domain]]
[[Category: Signaling protein]]
[[Category: Spermatogenesis]]
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