The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein.
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.
Boudko
Sergei P
SP
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2054, USA.
Kuhn
Richard J
RJ
Rossmann
Michael G
MG
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
D019590:Nucleocapsid Proteins; D011993:Recombinant Fusion Proteins