2gec: Difference between revisions

Revision as of 20:34, 28 July 2008

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File:2gec.png

Template:STRUCTURE 2gec

Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangementStructure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement

Template:ABSTRACT PUBMED 16775348

About this StructureAbout this Structure

2GEC is a Single protein structure of sequence from Infectious bronchitis virus. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structures of the N- and C-terminal domains of a coronavirus nucleocapsid protein: implications for nucleocapsid formation., Jayaram H, Fan H, Bowman BR, Ooi A, Jayaram J, Collisson EW, Lescar J, Prasad BV, J Virol. 2006 Jul;80(13):6612-20. PMID:16775348

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-'''Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement'''
+===Structure of the N-terminal domain of avian infectious bronchitis virus nucleocapsid protein (strain Gray) in a novel dimeric arrangement===
-==Overview==
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-Coronaviruses cause a variety of respiratory and enteric diseases in animals and humans including severe acute respiratory syndrome. In these enveloped viruses, the filamentous nucleocapsid is formed by the association of nucleocapsid (N) protein with single-stranded viral RNA. The N protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. We describe the structure of the two proteolytically resistant domains of the N protein from infectious bronchitis virus (IBV), a prototype coronavirus. These domains are located at its N- and C-terminal ends (NTD and CTD, respectively). The NTD of the IBV Gray strain at 1.3-A resolution exhibits a U-shaped structure, with two arms rich in basic residues, providing a module for specific interaction with RNA. The CTD forms a tightly intertwined dimer with an intermolecular four-stranded central beta-sheet platform flanked by alpha helices, indicating that the basic building block for coronavirus nucleocapsid formation is a dimeric assembly of N protein. The variety of quaternary arrangements of the NTD and CTD revealed by the analysis of the different crystal forms delineates possible interfaces that could be used for the formation of a flexible filamentous ribonucleocapsid. The striking similarity between the dimeric structure of CTD and the nucleocapsid-forming domain of a distantly related arterivirus indicates a conserved mechanism of nucleocapsid formation for these two viral families.
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+{{ABSTRACT_PUBMED_16775348}}
 ==About this Structure==
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 [[Category: N protein]]
 [[Category: Nucleocapsid protein]]
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