7c21
From Proteopedia
(Difference between revisions)
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==Crystal structure of Duvenhage virus phosphoprotein C-terminal domain== | ==Crystal structure of Duvenhage virus phosphoprotein C-terminal domain== | ||
- | <StructureSection load='7c21' size='340' side='right'caption='[[7c21]]' scene=''> | + | <StructureSection load='7c21' size='340' side='right'caption='[[7c21]], [[Resolution|resolution]] 1.95Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C21 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7c21]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Duvenhage_lyssavirus Duvenhage lyssavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C21 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C21 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=7c21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c21 OCA], [https://pdbe.org/7c21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c21 RCSB], [https://www.ebi.ac.uk/pdbsum/7c21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c21 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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=7c21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c21 OCA], [https://pdbe.org/7c21 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c21 RCSB], [https://www.ebi.ac.uk/pdbsum/7c21 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c21 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PHOSP_DUVV PHOSP_DUVV] Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Lyssavirus P protein is a multifunctional protein that interacts with numerous host-cell proteins. The C-terminal domain (CTD) of P is important for inhibition of JAK-STAT signaling enabling the virus to evade host immunity. Several regions on the surface of rabies virus P are reported to interact with host factors. Among them, an extended, discrete hydrophobic patch of P CTD is notable. Although structures of P CTD of two strains of rabies virus, and of mokola virus have been solved, the structure of P CTD for Duvenhage virus, which is functionally divergent from these species for immune evasion function, is not known. Here, we analyze the structures of P CTD of Duvenhage and of a distinct rabies virus strain to gain further insight on the nature and potential function of the hydrophobic surface. Molecular contacts in crystals suggest that the hydrophobic patch is important to intermolecular interactions with other proteins, which differ between the lyssavirus species. | ||
+ | |||
+ | Structural comparison of the C-terminal domain of functionally divergent lyssavirus P proteins.,Sugiyama A, Nomai T, Jiang X, Minami M, Yao M, Maenaka K, Ito N, Gooley PR, Moseley GW, Ose T Biochem Biophys Res Commun. 2020 Aug 20;529(2):507-512. doi:, 10.1016/j.bbrc.2020.05.195. Epub 2020 Jul 2. PMID:32703459<ref>PMID:32703459</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7c21" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Duvenhage lyssavirus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jiang X]] | [[Category: Jiang X]] |
Current revision
Crystal structure of Duvenhage virus phosphoprotein C-terminal domain
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