4a2v: Difference between revisions
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<StructureSection load='4a2v' size='340' side='right'caption='[[4a2v]], [[Resolution|resolution]] 1.44Å' scene=''> | <StructureSection load='4a2v' size='340' side='right'caption='[[4a2v]], [[Resolution|resolution]] 1.44Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a2v]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anapl Anapl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2V FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </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=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a2p|4a2p]], [[4a2x|4a2x]], [[4a36|4a36]], [[4a2q|4a2q]], [[4a2w|4a2w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a2p|4a2p]], [[4a2x|4a2x]], [[4a36|4a36]], [[4a2q|4a2q]], [[4a2w|4a2w]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2v OCA], [https://pdbe.org/4a2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2v RCSB], [https://www.ebi.ac.uk/pdbsum/4a2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Anapl]] | [[Category: Anapl]] | ||
[[Category: Large Structures]] | |||
[[Category: Cusack, S]] | [[Category: Cusack, S]] | ||
[[Category: Kowalinski, E]] | [[Category: Kowalinski, E]] | ||
Revision as of 10:41, 18 August 2022
Structure of duck RIG-I C-terminal domain (CTD)Structure of duck RIG-I C-terminal domain (CTD)
Structural highlights
Publication Abstract from PubMedRIG-I is a key innate immune pattern-recognition receptor that triggers interferon expression upon detection of intracellular 5'triphosphate double-stranded RNA (5'ppp-dsRNA) of viral origin. RIG-I comprises N-terminal caspase activation and recruitment domains (CARDs), a DECH helicase, and a C-terminal domain (CTD). We present crystal structures of the ligand-free, autorepressed, and RNA-bound, activated states of RIG-I. Inactive RIG-I has an open conformation with the CARDs sequestered by a helical domain inserted between the two helicase moieties. ATP and dsRNA binding induce a major rearrangement to a closed conformation in which the helicase and CTD bind the blunt end 5'ppp-dsRNA with perfect complementarity but incompatibly with continued CARD binding. We propose that after initial binding of 5'ppp-dsRNA to the flexibly linked CTD, co-operative tight binding of ATP and RNA to the helicase domain liberates the CARDs for downstream signaling. These findings significantly advance our molecular understanding of the activation of innate immune signaling helicases. Structural Basis for the Activation of Innate Immune Pattern-Recognition Receptor RIG-I by Viral RNA.,Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S Cell. 2011 Oct 14;147(2):423-35. PMID:22000019[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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