7qrx
From Proteopedia
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==Crystal structure of NHL domain of TRIM71== | ==Crystal structure of NHL domain of TRIM71== | ||
| - | <StructureSection load='7qrx' size='340' side='right'caption='[[7qrx]]' scene=''> | + | <StructureSection load='7qrx' size='340' side='right'caption='[[7qrx]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qrx]] 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=7QRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRX FirstGlance]. <br> |
| - | </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=7qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qrx OCA], [https://pdbe.org/7qrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qrx RCSB], [https://www.ebi.ac.uk/pdbsum/7qrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qrx ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=7qrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qrx OCA], [https://pdbe.org/7qrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qrx RCSB], [https://www.ebi.ac.uk/pdbsum/7qrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qrx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/LIN41_HUMAN LIN41_HUMAN] Congenital communicating hydrocephalus. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LIN41_HUMAN LIN41_HUMAN] E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (PubMed:28431233).[UniProtKB:Q1PSW8]<ref>PMID:23125361</ref> <ref>PMID:28431233</ref> <ref>PMID:24239284</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of the RING-type E3 ubiquitin ligases that play a role in diverse processes from homeostasis and immune response to viral restriction. While TRIM proteins typically harbor an N-terminal RING finger, a B-box and a coiled-coil domain, a high degree of diversity lies in their C termini that contain diverse protein interaction modules, most of which, both structures and their roles in intermolecular interactions, remain unknown. Here, high-resolution crystal structures of the NHL domains of three of the four human TRIM-NHL proteins, namely TRIM2, TRIM3 and TRIM71, are presented. Comparative structural analyses revealed that, despite sharing an evolutionarily conserved six-bladed beta-propeller architecture, the low sequence identities resulted in distinct properties of these interaction domains at their putative binding sites for macromolecules. Interestingly, residues lining the binding cavities represent a hotspot for genetic mutations linked to several diseases. Thus, high sequence diversity within the conserved NHL domains might be essential for differentiating binding partners among TRIM-NHL proteins. | ||
| + | |||
| + | Comparative structural analyses of the NHL domains from the human E3 ligase TRIM-NHL family.,Chaikuad A, Zhubi R, Tredup C, Knapp S IUCrJ. 2022 Sep 27;9(Pt 6):720-727. doi: 10.1107/S2052252522008582. eCollection , 2022 Nov 1. PMID:36381143<ref>PMID:36381143</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7qrx" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chaikuad A]] | [[Category: Chaikuad A]] | ||
[[Category: Knapp S]] | [[Category: Knapp S]] | ||
Revision as of 10:18, 14 December 2022
Crystal structure of NHL domain of TRIM71
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