6gfj: Difference between revisions

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'''Unreleased structure'''


The entry 6gfj is ON HOLD
==Structure of RIP2 CARD domain fused to crystallisable MBP tag==
<StructureSection load='6gfj' size='340' side='right'caption='[[6gfj]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gfj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GFJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gfj OCA], [http://pdbe.org/6gfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gfj RCSB], [http://www.ebi.ac.uk/pdbsum/6gfj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gfj ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Activation of the innate immune pattern recognition receptor NOD2 by the bacterial muramyl-dipeptide peptidoglycan fragment triggers recruitment of the downstream adaptor kinase RIP2, eventually leading to NF-kappaB activation and proinflammatory cytokine production. Here we show that full-length RIP2 can form long filaments mediated by its caspase recruitment domain (CARD), in common with other innate immune adaptor proteins. We further show that the NOD2 tandem CARDs bind to one end of the RIP2 CARD filament, suggesting a mechanism for polar filament nucleation by activated NOD2. We combine X-ray crystallography, solid-state NMR and high-resolution cryo-electron microscopy to determine the atomic structure of the helical RIP2 CARD filament, which reveals the intermolecular interactions that stabilize the assembly. Using structure-guided mutagenesis, we demonstrate the importance of RIP2 polymerization for the activation of NF-kappaB signalling by NOD2. Our results could be of use to develop new pharmacological strategies to treat inflammatory diseases characterised by aberrant NOD2 signalling.


Authors: Pellegrini, E., Cusack, S.
RIP2 filament formation is required for NOD2 dependent NF-kappaB signalling.,Pellegrini E, Desfosses A, Wallmann A, Schulze WM, Rehbein K, Mas P, Signor L, Gaudon S, Zenkeviciute G, Hons M, Malet H, Gutsche I, Sachse C, Schoehn G, Oschkinat H, Cusack S Nat Commun. 2018 Oct 2;9(1):4043. doi: 10.1038/s41467-018-06451-3. PMID:30279485<ref>PMID:30279485</ref>


Description: Structure of RIP2 CARD domain fused to crystallisable MBP tag
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6gfj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cusack, S]]
[[Category: Cusack, S]]
[[Category: Pellegrini, E]]
[[Category: Pellegrini, E]]
[[Category: Card]]
[[Category: Crystallographic mbp]]
[[Category: Death domain]]
[[Category: Rip2]]
[[Category: Transferase]]

Latest revision as of 12:01, 13 March 2019

Structure of RIP2 CARD domain fused to crystallisable MBP tag

6gfj, resolution 3.30Å

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