5chv
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of USP18-ISG15 complex== | |
- | + | <StructureSection load='5chv' size='340' side='right' caption='[[5chv]], [[Resolution|resolution]] 3.00Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5chv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHV FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
- | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr> |
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cht|5cht]]</td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chv OCA], [http://pdbe.org/5chv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chv RCSB], [http://www.ebi.ac.uk/pdbsum/5chv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5chv ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/UBP18_MOUSE UBP18_MOUSE]] Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms (By similarity). [[http://www.uniprot.org/uniprot/ISG15_MOUSE ISG15_MOUSE]] Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Can also isgylate: DDX58/RIG-I which inhibits its function in antiviral signaling response and EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A and B virus, sindbis virus (SV) and herpes simplex type-1 (HHV-1). Plays a significant role in the control of neonatal Chikungunya virus (CHIKV) infection by acting as a putative immunomodulator of proinflammatory cytokines. Protects mice against the consequences of Chikungunya virus infection by downregulating the pathogenic cytokine response, often denoted as the cytokine storm. Plays a role in erythroid differentiation. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity.<ref>PMID:16254333</ref> <ref>PMID:17222803</ref> <ref>PMID:17227866</ref> <ref>PMID:17289916</ref> <ref>PMID:18057259</ref> <ref>PMID:22022510</ref> <ref>PMID:22028657</ref> <ref>PMID:22859821</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Basters, A]] | ||
[[Category: Fritz, G]] | [[Category: Fritz, G]] | ||
- | [[Category: | + | [[Category: Hydrolase]] |
+ | [[Category: Interferon]] | ||
+ | [[Category: Isg15]] | ||
+ | [[Category: Ubiquitin-specific protease]] |
Revision as of 17:01, 3 October 2016
Crystal structure of USP18-ISG15 complex
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