3hd4

<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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</td></tr>

[[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>

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== 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<ref>PMID:19782089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3hd4" style="background-color:#fffaf0;"></div>

[[Category: Cvma5]]

[[Category: Giedroc, D P]]

[[Category: III, C E.Dann]]

[[Category: Keane, S C]]

[[Category: Beta platform beta hairpin]]

[[Category: Virion]]