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| | <StructureSection load='6jbm' size='340' side='right'caption='[[6jbm]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6jbm' size='340' side='right'caption='[[6jbm]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jbm]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JBM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jbm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JBM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=6jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbm OCA], [http://pdbe.org/6jbm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jbm RCSB], [http://www.ebi.ac.uk/pdbsum/6jbm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbm ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6jbm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbm OCA], [https://pdbe.org/6jbm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jbm RCSB], [https://www.ebi.ac.uk/pdbsum/6jbm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRI14_HUMAN TRI14_HUMAN]] Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593).<ref>PMID:24379373</ref> <ref>PMID:27666593</ref> <ref>PMID:29053956</ref> | + | [https://www.uniprot.org/uniprot/TRI14_HUMAN TRI14_HUMAN] Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593).<ref>PMID:24379373</ref> <ref>PMID:27666593</ref> <ref>PMID:29053956</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6jbm" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6jbm" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liang, L]] | + | [[Category: Liang L]] |
| - | [[Category: Yin, Y X]] | + | [[Category: Yin YX]] |
| - | [[Category: Yu, Y]] | + | [[Category: Yu Y]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein interaction domain]]
| + | |
| - | [[Category: Trim]]
| + | |
| Structural highlights
Function
TRI14_HUMAN Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593).[1] [2] [3]
Publication Abstract from PubMed
Tripartite motif (TRIM)14 was recently shown to be an important molecule against pathogens. Its PRYSPRY domain acts as a protein-protein interaction module. TRIM14 exerts distinct functions via its PRYSPRY domain by interacting with different partners. However, the structural basis for its binding specificity remains unknown. Here we solved the crystal structure of the TRIM14 PRYSPRY domain, and found a positively charged surface that may mediate its partner specificity. Isothermal titration calorimetry reveals that the TRIM14 PRYSPRY domain binds to acidic peptides, and the analysis of the reported partners of TRIM14 is consistent with our assumption. Therefore, we demonstrate that the PRYSPRY domain of TRIM14 harbors a putative basic interface that may favorably bind to acidic amino acid residues.
The TRIM14 PRYSPRY domain mediates protein interaction via its basic interface.,Yu Y, Liang L, Jin Y, Yin Y FEBS Lett. 2019 May;593(10):1122-1129. doi: 10.1002/1873-3468.13386. Epub 2019, Apr 24. PMID:30973643[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou Z, Jia X, Xue Q, Dou Z, Ma Y, Zhao Z, Jiang Z, He B, Jin Q, Wang J. TRIM14 is a mitochondrial adaptor that facilitates retinoic acid-inducible gene-I-like receptor-mediated innate immune response. Proc Natl Acad Sci U S A. 2014 Jan 14;111(2):E245-54. doi:, 10.1073/pnas.1316941111. Epub 2013 Dec 30. PMID:24379373 doi:http://dx.doi.org/10.1073/pnas.1316941111
- ↑ Chen M, Meng Q, Qin Y, Liang P, Tan P, He L, Zhou Y, Chen Y, Huang J, Wang RF, Cui J. TRIM14 Inhibits cGAS Degradation Mediated by Selective Autophagy Receptor p62 to Promote Innate Immune Responses. Mol Cell. 2016 Oct 6;64(1):105-119. doi: 10.1016/j.molcel.2016.08.025. Epub 2016 , Sep 22. PMID:27666593 doi:http://dx.doi.org/10.1016/j.molcel.2016.08.025
- ↑ Tan P, He L, Cui J, Qian C, Cao X, Lin M, Zhu Q, Li Y, Xing C, Yu X, Wang HY, Wang RF. Assembly of the WHIP-TRIM14-PPP6C Mitochondrial Complex Promotes RIG-I-Mediated Antiviral Signaling. Mol Cell. 2017 Oct 19;68(2):293-307.e5. doi: 10.1016/j.molcel.2017.09.035. PMID:29053956 doi:http://dx.doi.org/10.1016/j.molcel.2017.09.035
- ↑ Yu Y, Liang L, Jin Y, Yin Y. The TRIM14 PRYSPRY domain mediates protein interaction via its basic interface. FEBS Lett. 2019 May;593(10):1122-1129. doi: 10.1002/1873-3468.13386. Epub 2019, Apr 24. PMID:30973643 doi:http://dx.doi.org/10.1002/1873-3468.13386
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