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| | ==crystal structure of horse MAVS card domain mutant E26R== | | ==crystal structure of horse MAVS card domain mutant E26R== |
| - | <StructureSection load='4o9l' size='340' side='right' caption='[[4o9l]], [[Resolution|resolution]] 1.94Å' scene=''> | + | <StructureSection load='4o9l' size='340' side='right'caption='[[4o9l]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o9l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o9l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9L FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o9f|4o9f]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.944Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAVS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=4o9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9l OCA], [https://pdbe.org/4o9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9l RCSB], [https://www.ebi.ac.uk/pdbsum/4o9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9l ProSAT]</span></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=4o9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o9l RCSB], [http://www.ebi.ac.uk/pdbsum/4o9l PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4o9l" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| - | [[Category: He, X]] | + | [[Category: Large Structures]] |
| - | [[Category: Zhang, X]] | + | [[Category: He X]] |
| - | [[Category: Antiviral protein]] | + | [[Category: Zhang X]] |
| Structural highlights
Publication Abstract from PubMed
Mitochondrial antiviral signaling (MAVS) protein is required for innate immune responses against RNA viruses. In virus-infected cells MAVS forms prion-like aggregates to activate antiviral signaling cascades, but the underlying structural mechanism is unknown. Here we report cryo-electron microscopic structures of the helical filaments formed by both the N-terminal caspase activation and recruitment domain (CARD) of MAVS and a truncated MAVS lacking part of the proline-rich region and the C-terminal transmembrane domain. Both structures are left-handed three-stranded helical filaments, revealing specific interfaces between individual CARD subunits that are dictated by electrostatic interactions between neighboring strands and hydrophobic interactions within each strand. Point mutations at multiple locations of these two interfaces impaired filament formation and antiviral signaling. Super-resolution imaging of virus-infected cells revealed rod-shaped MAVS clusters on mitochondria. These results elucidate the structural mechanism of MAVS polymerization, and explain how an alpha-helical domain uses distinct chemical interactions to form self-perpetuating filaments. DOI: http://dx.doi.org/10.7554/eLife.01489.001.
Structural basis for the prion-like MAVS filaments in antiviral innate immunity.,Xu H, He X, Zheng H, Huang LJ, Hou F, Yu Z, de la Cruz MJ, Borkowski B, Zhang X, Chen ZJ, Jiang QX Elife. 2014 Jan 1;3:e01489. doi: 10.7554/eLife.01489. PMID:24569476[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu H, He X, Zheng H, Huang LJ, Hou F, Yu Z, de la Cruz MJ, Borkowski B, Zhang X, Chen ZJ, Jiang QX. Structural basis for the prion-like MAVS filaments in antiviral innate immunity. Elife. 2014 Jan 1;3:e01489. doi: 10.7554/eLife.01489. PMID:24569476
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