View source for 7x70


==TRIM7 in complex with C-terminal peptide of NSP8==
<StructureSection load='7x70' size='340' side='right'caption='[[7x70]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7x70]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7X70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X70 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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=7x70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x70 OCA], [https://pdbe.org/7x70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x70 RCSB], [https://www.ebi.ac.uk/pdbsum/7x70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x70 ProSAT]</span></td></tr>
</table>
== Function ==
[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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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7x70" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome coronavirus 2]]
[[Category: Li XZ]]
[[Category: Liang X]]
[[Category: Zhang H]]