7w0s

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==TRIM7 in complex with C-terminal peptide of 2C==
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<StructureSection load='7w0s' size='340' side='right'caption='[[7w0s]]' scene=''>
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<StructureSection load='7w0s' size='340' side='right'caption='[[7w0s]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7w0s]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Coxsackievirus Coxsackievirus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W0S FirstGlance]. <br>
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</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=7w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w0s OCA], [https://pdbe.org/7w0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w0s RCSB], [https://www.ebi.ac.uk/pdbsum/7w0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w0s ProSAT]</span></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7w0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w0s OCA], [https://pdbe.org/7w0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w0s RCSB], [https://www.ebi.ac.uk/pdbsum/7w0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w0s ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRIM7_HUMAN TRIM7_HUMAN] E3 ubiquitin-protein ligase. Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation (PubMed:25851810). Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of proinflammatory cytokines and type I interferon (By similarity). Plays also a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation (PubMed:32126128).[UniProtKB:Q923T7]<ref>PMID:25851810</ref> <ref>PMID:32126128</ref> (Microbial infection) Promotes Zika virus replication by mediating envelope protein E ubiquitination.<ref>PMID:32641828</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The E3 ligase TRIM7 has emerged as a critical player in viral infection and pathogenesis. However, the mechanism governing the TRIM7-substrate association remains to be defined. Here we report the crystal structures of TRIM7 in complex with 2C peptides of human enterovirus. Structure-guided studies reveal the C-terminal glutamine residue of 2C as the primary determinant for TRIM7 binding. Leveraged by this finding, we identify norovirus and SARS-CoV-2 proteins, and physiological proteins, as new TRIM7 substrates. Crystal structures of TRIM7 in complex with multiple peptides derived from SARS-CoV-2 proteins display the same glutamine-end recognition mode. Furthermore, TRIM7 could trigger the ubiquitination and degradation of these substrates, possibly representing a new Gln/C-degron pathway. Together, these findings unveil a common recognition mode by TRIM7, providing the foundation for further mechanistic characterization of antiviral and cellular functions of TRIM7.
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A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures.,Liang X, Xiao J, Li X, Liu Y, Lu Y, Wen Y, Li Z, Che X, Ma Y, Zhang X, Zhang Y, Jian D, Wang P, Xuan C, Yu G, Li L, Zhang H Nat Chem Biol. 2022 Aug 18. pii: 10.1038/s41589-022-01128-x. doi:, 10.1038/s41589-022-01128-x. PMID:35982226<ref>PMID:35982226</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7w0s" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Coxsackievirus]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Li XZ]]
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[[Category: Liang X]]
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[[Category: Zhang H]]

Revision as of 06:27, 26 October 2022

TRIM7 in complex with C-terminal peptide of 2C

PDB ID 7w0s

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