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| | ==MHV Nucleocapsid Protein NTD== | | ==MHV Nucleocapsid Protein NTD== |
| - | <StructureSection load='3hd4' size='340' side='right' caption='[[3hd4]], [[Resolution|resolution]] 1.75Å' scene=''> | + | <StructureSection load='3hd4' size='340' side='right'caption='[[3hd4]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hd4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HD4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HD4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hd4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HD4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HD4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N, 7a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N, 7a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd4 OCA], [http://pdbe.org/3hd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hd4 RCSB], [http://www.ebi.ac.uk/pdbsum/3hd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd4 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hd4 OCA], [https://pdbe.org/3hd4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hd4 RCSB], [https://www.ebi.ac.uk/pdbsum/3hd4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hd4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NCAP_CVMA5 NCAP_CVMA5]] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid. Interaction with the M protein leads to the formation of virus particles. Binds to cellular membranes and phospholipids. Elicits cell-mediated immunity. May play roles in viral transcription and translation, and/or replication. Induces transcription of the prothrombinase (FGL2) and elevates procoagulant activity.<ref>PMID:12594208</ref> | + | [[https://www.uniprot.org/uniprot/NCAP_CVMA5 NCAP_CVMA5]] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid. Interaction with the M protein leads to the formation of virus particles. Binds to cellular membranes and phospholipids. Elicits cell-mediated immunity. May play roles in viral transcription and translation, and/or replication. Induces transcription of the prothrombinase (FGL2) and elevates procoagulant activity.<ref>PMID:12594208</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Nucleoprotein|Nucleoprotein]] | + | *[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Cvma5]] | | [[Category: Cvma5]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Giedroc, D P]] | | [[Category: Giedroc, D P]] |
| | [[Category: III, C E.Dann]] | | [[Category: III, C E.Dann]] |
| Structural highlights
Function
[NCAP_CVMA5] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid. Interaction with the M protein leads to the formation of virus particles. Binds to cellular membranes and phospholipids. Elicits cell-mediated immunity. May play roles in viral transcription and translation, and/or replication. Induces transcription of the prothrombinase (FGL2) and elevates procoagulant activity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
All coronaviruses (CoVs), including the causative agent of severe acute respiratory syndrome (SARS), encode a nucleocapsid (N) protein that harbors two independent RNA binding domains of known structure, but poorly characterized RNA binding properties. We show here that the N-terminal domain (NTD) of N protein from mouse hepatitis virus (MHV), a virus most closely related to SARS-CoV, employs aromatic amino acid-nucleobase stacking interactions with a triple adenosine motif to mediate high-affinity binding to single-stranded RNAs containing the transcriptional regulatory sequence (TRS) or its complement (cTRS). Stoichiometric NTD fully unwinds a TRS-cTRS duplex that mimics a transiently formed transcription intermediate in viral subgenomic RNA synthesis. Mutation of the solvent-exposed Y127, positioned on the beta-platform surface of our 1.75 A structure, binds the TRS far less tightly and is severely crippled in its RNA unwinding activity. In contrast, the C-terminal domain (CTD) exhibits no RNA unwinding activity. Viruses harboring Y127A N mutation are strongly selected against and Y127A N does not support an accessory function in MHV replication. We propose that the helix melting activity of the coronavirus N protein NTD plays a critical accessory role in subgenomic RNA synthesis and other processes requiring RNA remodeling.
Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes.,Grossoehme NE, Li L, Keane SC, Liu P, Dann CE 3rd, Leibowitz JL, Giedroc DP J Mol Biol. 2009 Dec 4;394(3):544-57. Epub 2009 Sep 24. PMID:19782089[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ning Q, Lakatoo S, Liu M, Yang W, Wang Z, Phillips MJ, Levy GA. Induction of prothrombinase fgl2 by the nucleocapsid protein of virulent mouse hepatitis virus is dependent on host hepatic nuclear factor-4 alpha. J Biol Chem. 2003 May 2;278(18):15541-9. Epub 2003 Feb 19. PMID:12594208 doi:http://dx.doi.org/10.1074/jbc.M212806200
- ↑ Grossoehme NE, Li L, Keane SC, Liu P, Dann CE 3rd, Leibowitz JL, Giedroc DP. Coronavirus N protein N-terminal domain (NTD) specifically binds the transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA duplexes. J Mol Biol. 2009 Dec 4;394(3):544-57. Epub 2009 Sep 24. PMID:19782089 doi:10.1016/j.jmb.2009.09.040
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