4n1k

</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=4n1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1k OCA], [https://pdbe.org/4n1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1k RCSB], [https://www.ebi.ac.uk/pdbsum/4n1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1k ProSAT]</span></td></tr>

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== 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>

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== References ==

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