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.


7rup

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "7rup" [edit=sysop:move=sysop])
Current revision (09:30, 25 October 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 7rup is ON HOLD
+
==Structure of the human GIGYF2-TNRC6A complex==
 +
<StructureSection load='7rup' size='340' side='right'caption='[[7rup]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[7rup]] 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=7RUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RUP 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]] 1.23&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <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=7rup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rup OCA], [https://pdbe.org/7rup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rup RCSB], [https://www.ebi.ac.uk/pdbsum/7rup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rup ProSAT]</span></td></tr>
 +
</table>
 +
== Disease ==
 +
[https://www.uniprot.org/uniprot/GGYF2_HUMAN GGYF2_HUMAN] Young adult-onset Parkinsonism. Disease susceptibility may be associated with variations affecting the gene represented in this entry. Its association with Parkinson disease is however unclear. According to a number of studies, variations affecting this gene are not a frequent cause of Parkinson disease, suggesting that GIGYF2 does not play a major role in Parkinson disease etiology (PubMed:19279319, PubMed:19429085, PubMed:19638301, PubMed:19482505, PubMed:20004041, PubMed:19321232, PubMed:20060621).<ref>PMID:19279319</ref> <ref>PMID:19321232</ref> <ref>PMID:19429085</ref> <ref>PMID:19482505</ref> <ref>PMID:19638301</ref> <ref>PMID:20004041</ref> <ref>PMID:20060621</ref>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GGYF2_HUMAN GGYF2_HUMAN] Key component of the 4EHP-GYF2 complex, a multiprotein complex that acts as a repressor of translation initiation (PubMed:22751931). In 4EHP-GYF2 the complex, acts as a factor that bridges EIF4E2 to ZFP36/TTP, linking translation repression with mRNA decay (By similarity). May act cooperatively with GRB10 to regulate tyrosine kinase receptor signaling, including IGF1 and insulin receptors (PubMed:12771153).[UniProtKB:Q6Y7W8]<ref>PMID:12771153</ref> <ref>PMID:22751931</ref>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The GIGYF proteins interact with 4EHP and RNA-associated proteins to elicit transcript-specific translational repression. However, the mechanism by which the GIGYF1/2-4EHP complex is recruited to its target transcripts remain unclear. Here we report the crystal structures of the GYF domains from GIGYF1 and GIGYF2 in complex with proline-rich sequences from miRISC-binding proteins TNRC6C and TNRC6A, respectively. The TNRC6 proline-rich motifs bind to a conserved array of aromatic residues on the surface of the GIGYF1/2 GYF domain, thereby bridging 4EHP to Argonaute-miRNA complexes. Our structures also reveal a phenylalanine residue conserved from yeast to human GYF domains that contributes to GIGYF2 thermostability. The molecular details we outline here are likely to be conserved between GIGYF1/2 and other RNA-binding proteins to elicit 4EHP-mediated repression in different biological contexts.
-
Authors: Sobti, M., Mead, B.J., Igreja, C., Stewart, A.G., Christie, M.
+
Molecular basis for GIGYF-TNRC6 complex assembly.,Sobti M, Mead BJ, Stewart AG, Igreja C, Christie M RNA. 2023 Feb 28:rna.079596.123. doi: 10.1261/rna.079596.123. PMID:36854607<ref>PMID:36854607</ref>
-
Description: Structure of the human GIGYF2-TNRC6A complex
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Mead, B.J]]
+
<div class="pdbe-citations 7rup" style="background-color:#fffaf0;"></div>
-
[[Category: Christie, M]]
+
== References ==
-
[[Category: Sobti, M]]
+
<references/>
-
[[Category: Igreja, C]]
+
__TOC__
-
[[Category: Stewart, A.G]]
+
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Christie M]]
 +
[[Category: Igreja C]]
 +
[[Category: Mead BJ]]
 +
[[Category: Sobti M]]
 +
[[Category: Stewart AG]]

Current revision

Structure of the human GIGYF2-TNRC6A complex

PDB ID 7rup

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7rup"
Personal tools