This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4b8e

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 16:43, 4 August 2016

PRY-SPRY domain of Trim25

Structural highlights

4b8e is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRI25_MOUSE] Functions as an 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 (By similarity).

Publication Abstract from PubMed

Tripartite motif (TRIM) proteins primarily function as ubiquitin E3 ligases that regulate the innate immune response to infection. TRIM25 (also known as estrogen-responsive finger protein (Efp)) has been implicated in the regulation of estrogen receptor alpha signaling, and in the regulation of innate immune signaling via retinoic acid-inducible gene-I (RIG-I). RIG-I senses cytosolic viral RNA, and is subsequently ubiquitinated by TRIM25 at its N-terminal CARD domains, leading to type I interferon production. The interaction with RIG-I is dependent on the TRIM25 B30.2 domain, a protein interaction domain composed of the PRY and SPRY tandem sequence motifs. Here we present the 1.8 A crystal structure of the TRIM25 B30.2 domain, which exhibits a typical B30.2/SPRY domain fold comprising two N-terminal alpha-helices, thirteen beta-strands arranged into two beta-sheets, and loop regions of varying lengths. A comparison with other B30.2/SPRY structures and an analysis of the loop regions identified a putative binding pocket, which is likely to be involved in binding target proteins. This was supported by mutagenesis and functional analyses, which identified two key residues (Asp-488, Trp-621) in the TRIM25 B30.2 domain as being critical for binding to the RIG-I CARD domains.

Crystal Structure of the TRIM25 B30.2 (PRYSPRY) domain: A Key Component of Antiviral Signaling.,D'Cruz AA, Kershaw NJ, Chiang JJ, Wang MK, Nicola NA, Babon JJ, Gack MU, Nicholson SE Biochem J. 2013 Sep 10. PMID:24015671^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ D'Cruz AA, Kershaw NJ, Chiang JJ, Wang MK, Nicola NA, Babon JJ, Gack MU, Nicholson SE. Crystal Structure of the TRIM25 B30.2 (PRYSPRY) domain: A Key Component of Antiviral Signaling. Biochem J. 2013 Sep 10. PMID:24015671 doi:10.1042/BJ20121425

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4b8e"

@@ Line 1: / Line 1: @@
 ==PRY-SPRY domain of Trim25==
 <StructureSection load='4b8e' size='340' side='right' caption='[[4b8e]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4b8e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B8E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B8E 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=EDO:1,2-ETHANEDIOL'>EDO</scene></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=4b8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b8e RCSB], [http://www.ebi.ac.uk/pdbsum/4b8e PDBsum]</span></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=4b8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8e OCA], [http://pdbe.org/4b8e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b8e RCSB], [http://www.ebi.ac.uk/pdbsum/4b8e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b8e ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4b8e" style="background-color:#fffaf0;"></div>
 ==See Also==

4b8e

From Proteopedia

Revision as of 16:43, 4 August 2016

PRY-SPRY domain of Trim25

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox