3G80
Nodamura virus protein b2, RNA-binding domain
Summary for 3G80
| Entry DOI | 10.2210/pdb3g80/pdb |
| Descriptor | Protein B2 (2 entities in total) |
| Functional Keywords | rna-binding, viral protein, suppressor of rnai, rna interference |
| Biological source | Nodamura virus (NoV) |
| Total number of polymer chains | 2 |
| Total formula weight | 22273.53 |
| Authors | Korber, S.,Shaik Syed Ali, P.,Chen, J.C. (deposition date: 2009-02-11, release date: 2010-01-05, Last modification date: 2023-09-06) |
| Primary citation | Korber, S.,Shaik Syed Ali, P.,Chen, J.C. Structure of the RNA-Binding Domain of Nodamura Virus Protein B2, a Suppressor of RNA Interference. Biochemistry, 48:2307-2309, 2009 Cited by PubMed Abstract: 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. PubMed: 19249868DOI: 10.1021/bi900126s PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report






