4a2p: Difference between revisions
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='4a2p' size='340' side='right'caption='[[4a2p]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4a2p' size='340' side='right'caption='[[4a2p]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a2p]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a2p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2P FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</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=4a2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2p OCA], [https://pdbe.org/4a2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2p RCSB], [https://www.ebi.ac.uk/pdbsum/4a2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2p ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D3TI84_ANAPL D3TI84_ANAPL] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Anas platyrhynchos]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cusack | [[Category: Cusack S]] | ||
[[Category: Kowalinski | [[Category: Kowalinski E]] | ||
[[Category: Lunardi | [[Category: Lunardi T]] | ||
[[Category: McCarthy | [[Category: McCarthy AA]] | ||
Latest revision as of 13:45, 9 May 2024
Structure of duck RIG-I helicase domainStructure of duck RIG-I helicase domain
Structural highlights
FunctionPublication 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
|
| ||||||||||||||||