2ibl: Difference between revisions

Revision as of 18:50, 21 February 2008

Crystal structure of a helper molecule (HT-mf-thromb) based on mini-fibritin (mf) crystal structure (pdb:1OX3).

OverviewOverview

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.

About this StructureAbout this Structure

2IBL is a Single protein structure of sequence from Unidentified phage. Full crystallographic information is available from OCA.

ReferenceReference

The coiled-coil domain structure of the Sin Nombre virus nucleocapsid protein., Boudko SP, Kuhn RJ, Rossmann MG, J Mol Biol. 2007 Mar 9;366(5):1538-44. Epub 2006 Dec 23. PMID:17222867

Page seeded by OCA on Thu Feb 21 17:50:56 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Single protein]]
 [[Category: Unidentified phage]]
-[[Category: Boudko, S.P.]]
+[[Category: Boudko, S P.]]
-[[Category: Rossmann, M.G.]]
+[[Category: Rossmann, M G.]]
 [[Category: bacteriophage t4]]
 [[Category: foldon]]
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 [[Category: trimerization]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:38:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:56 2008''