title: The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein.
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.
authors.affiliation: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2054, USA.
authors.forename: Sergei P
authors.initials: SP
authors.lastname: Boudko
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Kuhn
authors.forename: Michael G
authors.initials: MG
authors.lastname: Rossmann
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008027:Light; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019590:Nucleocapsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D029261:Sin Nombre virus / Q000737:chemistry* / Q000648:ultrastructure
chemical_list: D019590:Nucleocapsid Proteins; D011993:Recombinant Fusion Proteins