Structural highlights
Function
[B2_NODAM] Binds double-strand RNA (dsRNA) with high affinity. Suppresses the host RNA silencing-based antiviral response.[1]
Publication Abstract from PubMed
Protein B2 from Nodamura virus (NMV B2), a member of the Nodavirus family, acts as a suppressor of RNA interference (RNAi). The N-terminal domain of NMV B2, consisting of residues 1-79, recognizes double-stranded RNA (dsRNA). The 2.5 A crystal structure of the RNA-binding domain of NMV B2 shows a dimeric, helical bundle structure. The structure shows a conserved set of RNA-binding residues compared with flock house virus B2, despite limited sequence identity. The crystal packing places the RNA-binding residues along one face of symmetry-related molecules, suggesting a potential platform for recognition of dsRNA.
Structure of the RNA-Binding Domain of Nodamura Virus Protein B2, a Suppressor of RNA Interference (dagger) , (double dagger).,Korber S, Shaik Syed Ali P, Chen JC Biochemistry. 2009 Mar 24;48(11):2307-9. PMID:19249868[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Korber S, Shaik Syed Ali P, Chen JC. Structure of the RNA-Binding Domain of Nodamura Virus Protein B2, a Suppressor of RNA Interference (dagger) , (double dagger). Biochemistry. 2009 Mar 24;48(11):2307-9. PMID:19249868 doi:10.1021/bi900126s
- ↑ Korber S, Shaik Syed Ali P, Chen JC. Structure of the RNA-Binding Domain of Nodamura Virus Protein B2, a Suppressor of RNA Interference (dagger) , (double dagger). Biochemistry. 2009 Mar 24;48(11):2307-9. PMID:19249868 doi:10.1021/bi900126s
