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| | ==Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein== | | ==Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein== |
| - | <StructureSection load='1ssk' size='340' side='right'caption='[[1ssk]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1ssk' size='340' side='right'caption='[[1ssk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ssk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SSK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ssk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SSK FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1ssk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssk OCA], [http://pdbe.org/1ssk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ssk RCSB], [http://www.ebi.ac.uk/pdbsum/1ssk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssk 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=1ssk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ssk OCA], [https://pdbe.org/1ssk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ssk RCSB], [https://www.ebi.ac.uk/pdbsum/1ssk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ssk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NCAP_CVHSA NCAP_CVHSA]] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid (By similarity). | + | [https://www.uniprot.org/uniprot/NCAP_SARS NCAP_SARS] Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455).[HAMAP-Rule:MF_04096]<ref>PMID:17210170</ref> <ref>PMID:18055455</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cvhsa]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fesik, S W]] | + | [[Category: Severe acute respiratory syndrome-related coronavirus]] |
| - | [[Category: Gunasekera, A]] | + | [[Category: Fesik SW]] |
| - | [[Category: Hajduk, P]] | + | [[Category: Gunasekera A]] |
| - | [[Category: Huang, Q]] | + | [[Category: Hajduk P]] |
| - | [[Category: Liu, Z]] | + | [[Category: Huang Q]] |
| - | [[Category: Mack, J]] | + | [[Category: Liu Z]] |
| - | [[Category: Olejniczak, E T]] | + | [[Category: Mack J]] |
| - | [[Category: Petros, A M]] | + | [[Category: Olejniczak ET]] |
| - | [[Category: Xu, N]] | + | [[Category: Petros AM]] |
| - | [[Category: Yu, L]] | + | [[Category: Xu N]] |
| - | [[Category: Nucleocapsid protein]]
| + | [[Category: Yu L]] |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
NCAP_SARS Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455).[HAMAP-Rule:MF_04096][1] [2]
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
The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site.
Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein.,Huang Q, Yu L, Petros AM, Gunasekera A, Liu Z, Xu N, Hajduk P, Mack J, Fesik SW, Olejniczak ET Biochemistry. 2004 May 25;43(20):6059-63. PMID:15147189[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stertz S, Reichelt M, Spiegel M, Kuri T, Martínez-Sobrido L, García-Sastre A, Weber F, Kochs G. The intracellular sites of early replication and budding of SARS-coronavirus. Virology. 2007 May 10;361(2):304-15. PMID:17210170 doi:10.1016/j.virol.2006.11.027
- ↑ Zhao X, Nicholls JM, Chen YG. Severe acute respiratory syndrome-associated coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling. J Biol Chem. 2008 Feb 8;283(6):3272-3280. PMID:18055455 doi:10.1074/jbc.M708033200
- ↑ Huang Q, Yu L, Petros AM, Gunasekera A, Liu Z, Xu N, Hajduk P, Mack J, Fesik SW, Olejniczak ET. Structure of the N-terminal RNA-binding domain of the SARS CoV nucleocapsid protein. Biochemistry. 2004 May 25;43(20):6059-63. PMID:15147189 doi:10.1021/bi036155b
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