1ssk: Difference between revisions
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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]], [[NMR_Ensembles_of_Models | 1 NMR models]]' 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:// | <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> | ||
</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='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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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: Cvhsa]] | [[Category: Cvhsa]] | ||
[[Category: Large Structures]] | |||
[[Category: Fesik, S W]] | [[Category: Fesik, S W]] | ||
[[Category: Gunasekera, A]] | [[Category: Gunasekera, A]] | ||
Revision as of 14:33, 24 December 2020
Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid ProteinStructure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein
Structural highlights
Function[NCAP_CVHSA] Major structural component of virions that associates with genomic RNA to form a long, flexible, helical nucleocapsid (By similarity). 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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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