ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A cryptic pocket in Ebola VP35 allosterically controls RNA binding.Nature communications · 2022Article
- Global phosphoproteomic analysis of Ebola virions reveals a novel role for VP35 phosphorylation-dependent regulation of genome transcription.Cellular and molecular life sciences : CMLS · 2020Article
- The Ebola Viral Protein 35 N-Terminus Is a Parallel Tetramer.Biochemistry · 2019Article
- In silico and in vitro methods to identify ebola virus VP35-dsRNA inhibitors.Bioorganic & medicinal chemistry · 2016Article
- Structural basis for Marburg virus VP35-mediated immune evasion mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- dsRNA binding characterization of full length recombinant wild type and mutants Zaire ebolavirus VP35.Antiviral research · 2012Article
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Authors and funding
12 authors.
Funding
Abstract
VP35 is one of seven structural proteins encoded by the Ebola viral genome and mediates viral replication, nucleocapsid formation and host immune suppression. The C-terminal interferon inhibitory domain (IID) of VP35 is critical for dsRNA binding and interferon inhibition. The wild-type VP35 IID structure revealed several conserved residues that are important for dsRNA binding and interferon antagonism. Here, the expression, purification and crystallization of recombinant Zaire Ebola VP35 IID mutants R312A, K319A/R322A and K339A in space groups P6(1)22, P2(1)2(1)2(1) and P2(1), respectively, are described. Diffraction data were collected using synchrotron sources at the Advanced Light Source and the Advanced Photon Source.
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