5i72
From Proteopedia
(Difference between revisions)
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<StructureSection load='5i72' size='340' side='right'caption='[[5i72]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='5i72' size='340' side='right'caption='[[5i72]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5i72]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5i72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lassj Lassj]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I72 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5i72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i72 OCA], [https://pdbe.org/5i72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i72 RCSB], [https://www.ebi.ac.uk/pdbsum/5i72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i72 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/Z_LASSJ Z_LASSJ]] Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L (By similarity). Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.<ref>PMID:12970458</ref> <ref>PMID:14990716</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 11:27, 23 March 2022
Crystal structure of the oligomeric form of the Lassa virus matrix protein Z
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Categories: Large Structures | Lassj | Hastie, K | Jr, V Woods | Li, S | Liu, T | Saphire, E O | Zandonatti, M | Arenavirus | Lassa virus | Matrix | Oligomer | Viral protein