The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein.

Boudko SP, Kuhn RJ, Rossmann MG
J Mol Biol. 2007 366 (5): 1538-44

PMID: 17222867 · PMCID: PMC1820746 · DOI:10.1016/j.jmb.2006.12.046

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.

MeSH Terms (16)

Amino Acid Sequence Crystallography, X-Ray Escherichia coli Humans Light Models, Biological Models, Molecular Molecular Sequence Data Nucleocapsid Proteins Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Recombinant Fusion Proteins Scattering, Radiation Sequence Homology, Amino Acid Sin Nombre virus

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