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3rc5
From Proteopedia
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{{STRUCTURE_3rc5| PDB=3rc5 | SCENE= }} | {{STRUCTURE_3rc5| PDB=3rc5 | SCENE= }} | ||
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===Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease=== | ===Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease=== | ||
| + | {{ABSTRACT_PUBMED_21507982}} | ||
| - | + | ==Function== | |
| - | + | [[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> | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:021507982</ref><references group="xtra"/> | + | <ref group="xtra">PMID:021507982</ref><references group="xtra"/><references/> |
[[Category: Hepatitis c virus subtype 1a]] | [[Category: Hepatitis c virus subtype 1a]] | ||
[[Category: Romano, K P.]] | [[Category: Romano, K P.]] | ||
[[Category: Schiffer, C A.]] | [[Category: Schiffer, C A.]] | ||
| + | [[Category: Drug design]] | ||
| + | [[Category: Drug resistance]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Protease inhibitor]] | ||
| + | [[Category: Serine protease]] | ||
Revision as of 08:10, 16 May 2013
Contents |
Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease
Template:ABSTRACT PUBMED 21507982
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]
About this Structure
3rc5 is a 2 chain structure with sequence from Hepatitis c virus subtype 1a. Full crystallographic information is available from OCA.
Reference
- Romano KP, Laine JM, Deveau LM, Cao H, Massi F, Schiffer CA. Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease. J Virol. 2011 Apr 20. PMID:21507982 doi:10.1128/JVI.00377-11
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
