2ms7: Difference between revisions

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'''Unreleased structure'''
==High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD==
 
<StructureSection load='2ms7' size='340' side='right' caption='[[2ms7]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
The entry 2ms7 is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2ms7]] is a 21 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MS7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MS7 FirstGlance]. <br>
Authors: He, L., Bardiaux, B., Spehr, J., Luehrs, T., Ritter, C.
</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=2ms7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ms7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ms7 RCSB], [http://www.ebi.ac.uk/pdbsum/2ms7 PDBsum]</span></td></tr>
 
</table>
Description: High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD
{{Large structure}}
[[Category: Unreleased Structures]]
== Function ==
[[Category: Spehr, J]]
[[http://www.uniprot.org/uniprot/MAVS_HUMAN MAVS_HUMAN]] Required for innate immune defense against viruses. Acts downstream of DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis.<ref>PMID:16125763</ref> <ref>PMID:16153868</ref> <ref>PMID:16177806</ref> <ref>PMID:16127453</ref> <ref>PMID:19631370</ref> <ref>PMID:20451243</ref> 
[[Category: Ritter, C]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bardiaux, B]]
[[Category: He, L]]
[[Category: He, L]]
[[Category: Luehrs, T]]
[[Category: Luehrs, T]]
[[Category: Bardiaux, B]]
[[Category: Ritter, C]]
[[Category: Spehr, J]]
[[Category: Mavs card filament]]
[[Category: Protein binding]]

Revision as of 15:28, 2 September 2015

High-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARDHigh-resolution solid-state NMR structure of the helical signal transduction filament MAVS CARD

Structural highlights

2ms7 is a 21 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum
Warning: this is a large structure, and loading might take a long time or not happen at all.

Function

[MAVS_HUMAN] Required for innate immune defense against viruses. Acts downstream of DDX58/RIG-I and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state. Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response. May activate the same pathways following detection of extracellular dsRNA by TLR3. May protect cells from apoptosis.[1] [2] [3] [4] [5] [6]

References

  1. ↑ Seth RB, Sun L, Ea CK, Chen ZJ. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3. Cell. 2005 Sep 9;122(5):669-82. PMID:16125763 doi:10.1016/j.cell.2005.08.012
  2. ↑ Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB. VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell. 2005 Sep 16;19(6):727-40. PMID:16153868 doi:S1097-2765(05)01556-X
  3. ↑ Meylan E, Curran J, Hofmann K, Moradpour D, Binder M, Bartenschlager R, Tschopp J. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature. 2005 Oct 20;437(7062):1167-72. Epub 2005 Sep 21. PMID:16177806 doi:nature04193
  4. ↑ Kawai T, Takahashi K, Sato S, Coban C, Kumar H, Kato H, Ishii KJ, Takeuchi O, Akira S. IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction. Nat Immunol. 2005 Oct;6(10):981-8. Epub 2005 Aug 28. PMID:16127453 doi:10.1038/ni1243
  5. ↑ Chiu YH, Macmillan JB, Chen ZJ. RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. doi: 10.1016/j.cell.2009.06.015. Epub 2009 Jul, 23. PMID:19631370 doi:10.1016/j.cell.2009.06.015
  6. ↑ Dixit E, Boulant S, Zhang Y, Lee AS, Odendall C, Shum B, Hacohen N, Chen ZJ, Whelan SP, Fransen M, Nibert ML, Superti-Furga G, Kagan JC. Peroxisomes are signaling platforms for antiviral innate immunity. Cell. 2010 May 14;141(4):668-81. doi: 10.1016/j.cell.2010.04.018. Epub 2010 May, 6. PMID:20451243 doi:10.1016/j.cell.2010.04.018
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