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- | {{Seed}} | |
- | [[Image:2ic6.png|left|200px]] | |
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- | <!--
| + | ==The Coiled-coil Domain (residues 1-75) Structure of the Sin Nombre Virus Nucleocapsid Protein== |
- | The line below this paragraph, containing "STRUCTURE_2ic6", creates the "Structure Box" on the page.
| + | <StructureSection load='2ic6' size='340' side='right'caption='[[2ic6]], [[Resolution|resolution]] 1.15Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2ic6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sin_Nombre_orthohantavirus Sin Nombre orthohantavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IC6 FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15Å</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=2ic6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ic6 OCA], [https://pdbe.org/2ic6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ic6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ic6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ic6 ProSAT]</span></td></tr> |
- | {{STRUCTURE_2ic6| PDB=2ic6 | SCENE= }}
| + | </table> |
- | | + | == Function == |
- | ===The Coiled-coil Domain (residues 1-75) Structure of the Sin Nombre Virus Nucleocapsid Protein===
| + | [https://www.uniprot.org/uniprot/NCAP_SINV NCAP_SINV] Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891).[UniProtKB:O36307][UniProtKB:P05133]<ref>PMID:15254200</ref> <ref>PMID:15650206</ref> <ref>PMID:16775315</ref> <ref>PMID:16971445</ref> <ref>PMID:18971945</ref> <ref>PMID:19047634</ref> <ref>PMID:20164193</ref> <ref>PMID:20844026</ref> <ref>PMID:21378500</ref> <ref>PMID:25062117</ref> <ref>PMID:27261891</ref> |
- | | + | == Evolutionary Conservation == |
- | | + | [[Image:Consurf_key_small.gif|200px|right]] |
- | <!-- | + | Check<jmol> |
- | The line below this paragraph, {{ABSTRACT_PUBMED_17222867}}, adds the Publication Abstract to the page
| + | <jmolCheckbox> |
- | (as it appears on PubMed at http://www.pubmed.gov), where 17222867 is the PubMed ID number.
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/2ic6_consurf.spt"</scriptWhenChecked> |
- | -->
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | {{ABSTRACT_PUBMED_17222867}}
| + | <text>to colour the structure by Evolutionary Conservation</text> |
- | | + | </jmolCheckbox> |
- | ==About this Structure== | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ic6 ConSurf]. |
- | 2IC6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sin_nombre_virus Sin nombre virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IC6 OCA].
| + | <div style="clear:both"></div> |
- | | + | == References == |
- | ==Reference== | + | <references/> |
- | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17222867 17222867]
| + | __TOC__ |
- | [[Category: Sin nombre virus]] | + | </StructureSection> |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Boudko, S P.]] | + | [[Category: Sin Nombre orthohantavirus]] |
- | [[Category: Rossmann, M G.]] | + | [[Category: Boudko SP]] |
- | [[Category: Antiparallel coiled coil]] | + | [[Category: Rossmann MG]] |
- | [[Category: Bunyaviridae]] | + | |
- | [[Category: Hantavirus]] | + | |
- | [[Category: Nucleocapsid protein]] | + | |
- | [[Category: Sin nombre virus]] | + | |
- | [[Category: Ssrna negative-strand viruse]] | + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:47:05 2008''
| + | |
| Structural highlights
Function
NCAP_SINV Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (PubMed:15650206, PubMed:15254200, PubMed:21378500, PubMed:16971445, PubMed:25062117, PubMed:16775315). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (PubMed:20164193). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (PubMed:19047634). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (PubMed:18971945, PubMed:25062117). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (PubMed:20844026, PubMed:20164193, PubMed:25062117). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (PubMed:27261891).[UniProtKB:O36307][UniProtKB:P05133][1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mir MA, Panganiban AT. Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle. J Virol. 2004 Aug;78(15):8281-8. PMID:15254200 doi:10.1128/JVI.78.15.8281-8288.2004
- ↑ Mir MA, Panganiban AT. The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding. J Virol. 2005 Feb;79(3):1824-35. PMID:15650206 doi:10.1128/JVI.79.3.1824-1835.2005
- ↑ Mir MA, Panganiban AT. Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein. J Virol. 2006 Jul;80(13):6276-85. PMID:16775315 doi:10.1128/JVI.00147-06
- ↑ Mir MA, Brown B, Hjelle B, Duran WA, Panganiban AT. Hantavirus N protein exhibits genus-specific recognition of the viral RNA panhandle. J Virol. 2006 Nov;80(22):11283-92. PMID:16971445 doi:10.1128/JVI.00820-06
- ↑ Mir MA, Panganiban AT. A protein that replaces the entire cellular eIF4F complex. EMBO J. 2008 Dec 3;27(23):3129-39. PMID:18971945 doi:10.1038/emboj.2008.228
- ↑ Mir MA, Duran WA, Hjelle BL, Ye C, Panganiban AT. Storage of cellular 5' mRNA caps in P bodies for viral cap-snatching. Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19294-9. PMID:19047634 doi:10.1073/pnas.0807211105
- ↑ Mir MA, Sheema S, Haseeb A, Haque A. Hantavirus nucleocapsid protein has distinct m7G cap J Biol Chem. 2010 Apr 9;285(15):11357-68. PMID:20164193 doi:10.1074/jbc.M110.102459
- ↑ Haque A, Mir MA. Interaction of hantavirus nucleocapsid protein with ribosomal protein S19. J Virol. 2010 Dec;84(23):12450-3. PMID:20844026 doi:10.1128/JVI.01388-10
- ↑ Brown BA, Panganiban AT. Identification of a region of hantavirus nucleocapsid protein required for RNA chaperone activity. RNA Biol. 2010 Nov-Dec;7(6):830-7. PMID:21378500 doi:10.4161/rna.7.6.13862
- ↑ Ganaie SS, Haque A, Cheng E, Bonny TS, Salim NN, Mir MA. Ribosomal protein S19-binding domain provides insights into hantavirus nucleocapsid protein-mediated translation initiation mechanism. Biochem J. 2014 Nov 15;464(1):109-21. PMID:25062117 doi:10.1042/BJ20140449
- ↑ Möncke-Buchner E, Szczepek M, Bokelmann M, Heinemann P, Raftery MJ, Krüger DH, Reuter M. Sin Nombre hantavirus nucleocapsid protein exhibits a metal-dependent DNA-specific endonucleolytic activity. Virology. 2016 Sep;496:67-76. PMID:27261891 doi:10.1016/j.virol.2016.05.009
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