4n1k: Difference between revisions

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== Function ==

[https://www.uniprot.org/uniprot/NAL14_HUMAN NAL14_HUMAN] May be involved in inflammation and spermatogenesis.

== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Pyrin domain|Pyrin domain]]

== References ==

__TOC__

</StructureSection>

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@@ Line 9: / Line 9: @@
 == 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 4n1k" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Pyrin domain|Pyrin domain]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>