7wbt: Difference between revisions
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New page: '''Unreleased structure''' The entry 7wbt is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of bovine NLRP9== | |||
<StructureSection load='7wbt' size='340' side='right'caption='[[7wbt]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WBT 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]] 2.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=7wbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wbt OCA], [https://pdbe.org/7wbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wbt RCSB], [https://www.ebi.ac.uk/pdbsum/7wbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wbt ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nucleotide-binding and oligomerisation domain-like receptors (NLRs) can form inflammasomes that activate caspase-1 and pro-interleukin-1beta and induce pyroptosis. NLR family pyrin domain-containing 9 (NLRP9) forms an inflammasome and activates innate immune responses during virus infection, but little is known about this process. Here, we report the crystal and cryo-electron microscopy structures of NLRP9 in an ADP-bound state, revealing inactive and closed conformations of NLRP9 and its similarities to other structurally characterised NLRs. Moreover, we found a C-terminal region interacting with the concave surface of the leucine-rich repeat domain of NLRP9. This region is unique among NLRs and might be involved in the specific function of NLRP9. These data provide the structural basis for understanding the mechanism of NLRP9 regulation and activation. | |||
The structure of NLRP9 reveals a unique C-terminal region with putative regulatory function.,Kamitsukasa Y, Nakano K, Murakami K, Hirata K, Yamamoto M, Shimizu T, Ohto U FEBS Lett. 2022 Jan 28. doi: 10.1002/1873-3468.14302. PMID:35090055<ref>PMID:35090055</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7wbt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Kamitsukasa Y]] | |||
[[Category: Ohto U]] | |||
[[Category: Shimizu T]] | |||
Latest revision as of 11:46, 30 October 2024
Crystal structure of bovine NLRP9
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