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8bs7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Multimerisation domain of Borna disease virus 1== | |
| + | <StructureSection load='8bs7' size='340' side='right'caption='[[8bs7]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8bs7]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Borna_disease_virus_1 Borna disease virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BS7 FirstGlance]. <br> | ||
| + | </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=8bs7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bs7 OCA], [https://pdbe.org/8bs7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bs7 RCSB], [https://www.ebi.ac.uk/pdbsum/8bs7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bs7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHOSP_BDVV PHOSP_BDVV] Essential component of the RNA polymerase transcription and replication complex. Acts as a scaffold which brings L in close proximity to the N-RNA complex. Plays a role in the segregation of the viral genome in host daughter cells during mitosis by interacting with host HMGB1, a host chromatin-remodeling DNA architectural protein, thereby stabilizing RNP on chromosomes. Interacts with host TBK1 and thus interferes with activation of cellular antiviral state. Inhibits cellular histone acetyltransferase activities.[UniProtKB:P0C798]<ref>PMID:15509569</ref> <ref>PMID:22607802</ref> <ref>PMID:25810554</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bornaviruses are RNA viruses with a mammalian, reptilian, and avian host range. The viruses infect neuronal cells and in rare cases cause a lethal encephalitis. The family Bornaviridae are part of the Mononegavirales order of viruses, which contain a nonsegmented viral genome. Mononegavirales encode a viral phosphoprotein (P) that binds both the viral polymerase (L) and the viral nucleoprotein (N). The P protein acts as a molecular chaperone and is required for the formation of a functional replication/transcription complex. In this study, the structure of the oligomerization domain of the phosphoprotein determined by X-ray crystallography is reported. The structural results are complemented with biophysical characterization using circular dichroism, differential scanning calorimetry and small-angle X-ray scattering. The data reveal the phosphoprotein to assemble into a stable tetramer, with the regions outside the oligomerization domain remaining highly flexible. A helix-breaking motif is observed between the alpha-helices at the midpoint of the oligomerization domain that appears to be conserved across the Bornaviridae. These data provide information on an important component of the bornavirus replication complex. | ||
| - | + | Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein.,Whitehead JD, Grimes JM, Keown JR Acta Crystallogr F Struct Biol Commun. 2023 Mar 1;79(Pt 3):51-60. doi: , 10.1107/S2053230X23000717. Epub 2023 Feb 23. PMID:36862093<ref>PMID:36862093</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8bs7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Borna disease virus 1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Grimes JM]] | ||
| + | [[Category: Keown JR]] | ||
| + | [[Category: Whitehead JD]] | ||
Current revision
Multimerisation domain of Borna disease virus 1
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