4ltb: Difference between revisions

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<StructureSection load='4ltb' size='340' side='right'caption='[[4ltb]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
<StructureSection load='4ltb' size='340' side='right'caption='[[4ltb]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ltb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LTB FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ltb]] is a 2 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=4LTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LTB FirstGlance]. <br>
</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=4ltb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ltb OCA], [http://pdbe.org/4ltb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ltb RCSB], [http://www.ebi.ac.uk/pdbsum/4ltb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ltb ProSAT]</span></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]] 2.59&#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=4ltb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ltb OCA], [https://pdbe.org/4ltb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ltb RCSB], [https://www.ebi.ac.uk/pdbsum/4ltb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ltb ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/TRI25_HUMAN TRI25_HUMAN] Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs.<ref>PMID:16352599</ref> <ref>PMID:17069755</ref> <ref>PMID:17392790</ref>  
Tripartite motif (TRIM) proteins make up a large family of coiled-coil-containing RING E3 ligases that function in many cellular processes, particularly innate antiviral response pathways. Both dimerization and higher-order assembly are important elements of TRIM protein function, but the atomic details of TRIM tertiary and quaternary structure have not been fully understood. Here, we present crystallographic and biochemical analyses of the TRIM coiled-coil and show that TRIM proteins dimerize by forming interdigitating antiparallel helical hairpins that position the N-terminal catalytic RING domains at opposite ends of the dimer and the C-terminal substrate-binding domains at the center. The dimer core comprises an antiparallel coiled-coil with a distinctive, symmetric pattern of flanking heptad and central hendecad repeats that appear to be conserved across the entire TRIM family. Our studies reveal how the coiled-coil organizes TRIM25 to polyubiquitylate the RIG-I/viral RNA recognition complex and how dimers of the TRIM5alpha protein are arranged within hexagonal arrays that recognize the HIV-1 capsid lattice and restrict retroviral replication.
 
The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.,Sanchez JG, Okreglicka K, Chandrasekaran V, Welker JM, Sundquist WI, Pornillos O Proc Natl Acad Sci U S A. 2014 Feb 18;111(7):2494-9. doi:, 10.1073/pnas.1318962111. Epub 2014 Feb 3. PMID:24550273<ref>PMID:24550273</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ltb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Okreglicka, K]]
[[Category: Okreglicka K]]
[[Category: Pornillos, O]]
[[Category: Pornillos O]]
[[Category: Sanchez, J G]]
[[Category: Sanchez JG]]
[[Category: Coiled-coil]]
[[Category: Metal binding protein]]

Latest revision as of 15:21, 1 March 2024

Coiled-coil domain of TRIM25Coiled-coil domain of TRIM25

Structural highlights

4ltb is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.59Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRI25_HUMAN Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase. Involved in innate immune defense against viruses by mediating ubiquitination of DDX58. Mediates 'Lys-63'-linked polyubiquitination of the DDX58 N-terminal CARD-like region which is crucial for triggering the cytosolic signal transduction that leads to the production of interferons in response to viral infection. Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway. Mediates estrogen action in various target organs.[1] [2] [3]

See Also

References

  1. ↑ Zou W, Zhang DE. The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase. J Biol Chem. 2006 Feb 17;281(7):3989-94. Epub 2005 Dec 13. PMID:16352599 doi:http://dx.doi.org/10.1074/jbc.M510787200
  2. ↑ Nakasato N, Ikeda K, Urano T, Horie-Inoue K, Takeda S, Inoue S. A ubiquitin E3 ligase Efp is up-regulated by interferons and conjugated with ISG15. Biochem Biophys Res Commun. 2006 Dec 15;351(2):540-6. Epub 2006 Oct 18. PMID:17069755 doi:http://dx.doi.org/10.1016/j.bbrc.2006.10.061
  3. ↑ Gack MU, Shin YC, Joo CH, Urano T, Liang C, Sun L, Takeuchi O, Akira S, Chen Z, Inoue S, Jung JU. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature. 2007 Apr 19;446(7138):916-920. PMID:17392790 doi:http://dx.doi.org/10.1038/nature05732

4ltb, resolution 2.59Å

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