期刊
BIOCHEMISTRY
卷 48, 期 11, 页码 2307-2309出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi900126s
关键词
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资金
- DFG [SFB 579]
- Hessian Ministry for Science and Culture
- Center for Membrane Proteomics
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 angstrom 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.
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