3l32
From Proteopedia
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==Structure of the dimerisation domain of the rabies virus phosphoprotein== | ==Structure of the dimerisation domain of the rabies virus phosphoprotein== | ||
| - | <StructureSection load='3l32' size='340' side='right' caption='[[3l32]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='3l32' size='340' side='right'caption='[[3l32]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3l32]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3l32]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rabies_virus_China/MRV Rabies virus China/MRV]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L32 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3l32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l32 OCA], [https://pdbe.org/3l32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l32 RCSB], [https://www.ebi.ac.uk/pdbsum/3l32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l32 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/PHOSP_RABVR PHOSP_RABVR] 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. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/3l32_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l3/3l32_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l32 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l32 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two alpha-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimerization domain of the vesicular stomatitis virus phosphoprotein and also from the tetramerization domain of the Sendai virus phosphoprotein, suggesting that oligomerization is conserved but not structure. | ||
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| - | Structure of the dimerization domain of the rabies virus phosphoprotein.,Ivanov I, Crepin T, Jamin M, Ruigrok RW J Virol. 2010 Apr;84(7):3707-10. Epub 2010 Jan 20. PMID:20089657<ref>PMID:20089657</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3l32" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Crepin | + | [[Category: Rabies virus China/MRV]] |
| - | [[Category: Ivanov | + | [[Category: Crepin T]] |
| - | [[Category: Jamin | + | [[Category: Ivanov I]] |
| - | [[Category: Ruigrok | + | [[Category: Jamin M]] |
| - | + | [[Category: Ruigrok RWH]] | |
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Current revision
Structure of the dimerisation domain of the rabies virus phosphoprotein
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