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7rup

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==Structure of the human GIGYF2-TNRC6A complex==
==Structure of the human GIGYF2-TNRC6A complex==
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<StructureSection load='7rup' size='340' side='right'caption='[[7rup]]' scene=''>
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<StructureSection load='7rup' size='340' side='right'caption='[[7rup]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>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>
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<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>
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</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>
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</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>
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<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>
</table>
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== Disease ==
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[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>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7rup" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Christie M]]
[[Category: Christie M]]

Revision as of 10:01, 15 March 2023

Structure of the human GIGYF2-TNRC6A complex

PDB ID 7rup

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