2ca1

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(New page: 200px<br /><applet load="2ca1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ca1, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:2ca1.gif|left|200px]]<br /><applet load="2ca1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ca1, resolution 2.6&Aring;" />
caption="2ca1, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF THE IBV CORONAVIRUS NUCLEOCAPSID'''<br />
'''CRYSTAL STRUCTURE OF THE IBV CORONAVIRUS NUCLEOCAPSID'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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2CA1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Infectious_bronchitis_virus Infectious bronchitis virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CA1 OCA].
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2CA1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Infectious_bronchitis_virus Infectious bronchitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA1 OCA].
==Reference==
==Reference==
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[[Category: Infectious bronchitis virus]]
[[Category: Infectious bronchitis virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bowman, B.R.]]
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[[Category: Bowman, B R.]]
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[[Category: Collison, E.W.]]
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[[Category: Collison, E W.]]
[[Category: Fan, H.]]
[[Category: Fan, H.]]
[[Category: Jayaram, H.]]
[[Category: Jayaram, H.]]
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[[Category: Lescar, J.]]
[[Category: Lescar, J.]]
[[Category: Ooi, A.]]
[[Category: Ooi, A.]]
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[[Category: Prasad, B.V.V.]]
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[[Category: Prasad, B V.V.]]
[[Category: nucleocapsid protein]]
[[Category: nucleocapsid protein]]
[[Category: viral nucleoprotein]]
[[Category: viral nucleoprotein]]
[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:03:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:32 2008''

Revision as of 14:46, 21 February 2008


2ca1, resolution 2.6Å

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CRYSTAL STRUCTURE OF THE IBV CORONAVIRUS NUCLEOCAPSID

Overview

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.

About this Structure

2CA1 is a Single protein structure of sequence from Infectious bronchitis virus. Full crystallographic information is available from OCA.

Reference

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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