4p4h
From Proteopedia
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| - | ''' | + | ==Caught-in-action signaling complex of RIG-I 2CARD domain and MAVS CARD domain== |
| + | <StructureSection load='4p4h' size='340' side='right' caption='[[4p4h]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p4h]] is a 21 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P4H FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p4h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p4h RCSB], [http://www.ebi.ac.uk/pdbsum/4p4h PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RIG-I activates interferon signaling pathways by promoting filament formation of the adaptor molecule, MAVS. Assembly of the MAVS filament is mediated by its CARD domain (CARDMAVS), and requires its interaction with the tandem CARDs of RIG-I (2CARDRIG-I). However, the precise nature of the interaction between 2CARDRIG-I and CARDMAVS, and how this interaction leads to CARDMAVS filament assembly, has been unclear. Here we report a 3.6 A electron microscopy structure of the CARDMAVS filament and a 3.4 A crystal structure of the 2CARDRIG-I:CARDMAVS complex, representing 2CARDRIG-I "caught in the act" of nucleating the CARDMAVS filament. These structures, together with functional analyses, show that 2CARDRIG-I acts as a template for the CARDMAVS filament assembly, by forming a helical tetrameric structure and recruiting CARDMAVS along its helical trajectory. Our work thus reveals that signal activation by RIG-I occurs by imprinting its helical assembly architecture on MAVS, a previously uncharacterized mechanism of signal transmission. | ||
| - | + | Molecular Imprinting as a Signal-Activation Mechanism of the Viral RNA Sensor RIG-I.,Wu B, Peisley A, Tetrault D, Li Z, Egelman EH, Magor KE, Walz T, Penczek PA, Hur S Mol Cell. 2014 Jul 9. pii: S1097-2765(14)00492-4. doi:, 10.1016/j.molcel.2014.06.010. PMID:25018021<ref>PMID:25018021</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: RNA helicase]] | ||
| + | [[Category: Hur, S.]] | ||
| + | [[Category: Wu, B.]] | ||
| + | [[Category: Signaling complex]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 07:33, 30 July 2014
Caught-in-action signaling complex of RIG-I 2CARD domain and MAVS CARD domain
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