Title of article :
The Coiled-coil Domain Structure of the Sin Nombre Virus Nucleocapsid Protein
Author/Authors :
Sergei P. Boudko، نويسنده , , Richard J. Kuhn and Michael G. Rossmann، نويسنده , , Michael G. Rossmann، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
7
From page :
1538
To page :
1544
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.
Keywords :
crystal structure , Sin Nombre virus , antiparallel coiled coil , hantavirus , mini-fibritin
Journal title :
Journal of Molecular Biology
Serial Year :
2007
Journal title :
Journal of Molecular Biology
Record number :
1249121
Link To Document :
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