4n1j
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4n1j is ON HOLD until Paper Publication Authors: Eibl, C., Hessenberger, M., Wenger, J., Brandstetter, H. Description: Crystal structures of NLRP14...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions== | |
| + | <StructureSection load='4n1j' size='340' side='right'caption='[[4n1j]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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> | ||
| + | <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> | ||
| + | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4n1j" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Pyrin domain|Pyrin domain]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brandstetter H]] | ||
| + | [[Category: Eibl C]] | ||
| + | [[Category: Hessenberger M]] | ||
| + | [[Category: Wenger J]] | ||
Current revision
Crystal structures of NLRP14 pyrin domain reveal a conformational switch mechanism, regulating its molecular interactions
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