2GTT
Crystal structure of the rabies virus nucleoprotein-RNA complex
Summary for 2GTT
| Entry DOI | 10.2210/pdb2gtt/pdb |
| Descriptor | Nucleoprotein, RNA (99-MER), PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | protein-rna complex, rabies virus, nucleoprotein, viral protein, rna binding protein |
| Biological source | Lyssavirus rabies More |
| Total number of polymer chains | 24 |
| Total formula weight | 1176436.18 |
| Authors | Albertini, A.A.V.,Wernimont, A.K.,Muziol, T.,Ravelli, R.B.G.,Weissenhorn, W.,Ruigrok, R.W.H. (deposition date: 2006-04-28, release date: 2006-09-19, Last modification date: 2023-10-18) |
| Primary citation | Albertini, A.A.V.,Wernimont, A.K.,Muziol, T.,Ravelli, R.B.G.,Clapier, C.R.,Schoehn, G.,Weissenhorn, W.,Ruigrok, R.W.H. Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex Science, 313:360-363, 2006 Cited by PubMed Abstract: Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle. PubMed: 16778023DOI: 10.1126/science.1125280 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.49 Å) |
Structure validation
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