2IC9
The Coiled-coil Domain (residues 1-93) Structure of the Sin Nombre Virus Nucleocapsid Protein
Summary for 2IC9
| Entry DOI | 10.2210/pdb2ic9/pdb |
| Related | 2IC6 |
| Descriptor | Nucleocapsid protein (2 entities in total) |
| Functional Keywords | sin nombre virus, hantavirus, bunyaviridae, ssrna negative-strand viruses, nucleocapsid protein, antiparallel coiled coil, viral protein |
| Biological source | Sin Nombre virus |
| Total number of polymer chains | 2 |
| Total formula weight | 21400.18 |
| Authors | Boudko, S.P.,Rossmann, M.G. (deposition date: 2006-09-12, release date: 2007-02-27, Last modification date: 2023-08-30) |
| Primary citation | Boudko, S.P.,Kuhn, R.J.,Rossmann, M.G. The Coiled-coil Domain Structure of the Sin Nombre Virus Nucleocapsid Protein. J.Mol.Biol., 366:1538-1544, 2007 Cited by PubMed Abstract: Hantaviruses can cause hemorrhagic fever with a renal syndrome and hantavirus pulmonary syndrome when transmitted to humans. The nucleocapsid protein of hantaviruses encapsidates viral genomic RNA and associates with transcription and replication complexes. Both the amino and carboxy termini of the nucleocapsid protein had been predicted to form trimers prior to the formation of the ribonucleoprotein. Crystal structures of amino-terminal fragments of the nucleocapsid protein showed the formation of intramolecular antiparallel coiled coils, but not intermolecular trimers. Thus, the amino-terminal part of the nucleocapsid protein is probably insufficient to initiate the trimerization of the full-length molecule. PubMed: 17222867DOI: 10.1016/j.jmb.2006.12.046 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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