4ibb: Difference between revisions
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{{STRUCTURE_4ibb| PDB=4ibb | SCENE= }} | {{STRUCTURE_4ibb| PDB=4ibb | SCENE= }} | ||
=== | ===Ebola virus VP35 bound to small molecule=== | ||
{{ABSTRACT_PUBMED_24495995}} | {{ABSTRACT_PUBMED_24495995}} | ||
Revision as of 12:55, 19 March 2014
Ebola virus VP35 bound to small moleculeEbola virus VP35 bound to small molecule
Template:ABSTRACT PUBMED 24495995
FunctionFunction
[VP35_EBOZM] Acsts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. The mechanism by which this blockage occurs remains incompletely defined, a hypothesis suggests that VP35 dsRNA-binding activity prevents activation of IRF3 by sequestering dsRNA. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR.[1] [2] [3] [4] [5]
About this StructureAbout this Structure
4ibb is a 2 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Brown CS, Lee MS, Leung DW, Wang T, Xu W, Luthra P, Anantpadma M, Shabman RS, Melito LM, Macmillan KS, Borek DM, Otwinowski Z, Ramanan P, Stubbs AJ, Peterson DS, Binning JM, Tonelli M, Olson MA, Davey R, Ready JM, Basler CF, Amarasinghe GK. In Silico Derived Small Molecules Bind the Filovirus VP35 Protein and Inhibit Its Polymerase Cofactor Activity. J Mol Biol. 2014 Feb 1. pii: S0022-2836(14)00048-5. doi:, 10.1016/j.jmb.2014.01.010. PMID:24495995 doi:http://dx.doi.org/10.1016/j.jmb.2014.01.010
- ↑ Muhlberger E, Weik M, Volchkov VE, Klenk HD, Becker S. Comparison of the transcription and replication strategies of marburg virus and Ebola virus by using artificial replication systems. J Virol. 1999 Mar;73(3):2333-42. PMID:9971816
- ↑ Basler CF, Wang X, Muhlberger E, Volchkov V, Paragas J, Klenk HD, Garcia-Sastre A, Palese P. The Ebola virus VP35 protein functions as a type I IFN antagonist. Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12289-94. PMID:11027311 doi:10.1073/pnas.220398297
- ↑ Basler CF, Mikulasova A, Martinez-Sobrido L, Paragas J, Muhlberger E, Bray M, Klenk HD, Palese P, Garcia-Sastre A. The Ebola virus VP35 protein inhibits activation of interferon regulatory factor 3. J Virol. 2003 Jul;77(14):7945-56. PMID:12829834
- ↑ Enterlein S, Warfield KL, Swenson DL, Stein DA, Smith JL, Gamble CS, Kroeker AD, Iversen PL, Bavari S, Muhlberger E. VP35 knockdown inhibits Ebola virus amplification and protects against lethal infection in mice. Antimicrob Agents Chemother. 2006 Mar;50(3):984-93. PMID:16495261 doi:10.1128/AAC.50.3.984-993.2006
- ↑ Feng Z, Cerveny M, Yan Z, He B. The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR. J Virol. 2007 Jan;81(1):182-92. Epub 2006 Oct 25. PMID:17065211 doi:JVI.01006-06
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Amarasinghe, G K.
- Binning, J M.
- Borek, D M.
- Brown, C S.
- CSGID, Center for Structural Genomics of Infectious Diseases.
- Leung, D W.
- Otwinowski, Z.
- Peterson, D S
- Ramanan, P.
- Stubbs, A J.
- Xu, W.
- Center for structural genomics of infectious disease
- Csgid
- Interferon inhibitory domain
- National institute of allergy and infectious disease
- Niaid
- Structural genomic
- Transcription-transcription inhibitor complex