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7qrv
From Proteopedia
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==Crystal structure of NHL domain of TRIM2 (full C-terminal)== | ==Crystal structure of NHL domain of TRIM2 (full C-terminal)== | ||
| - | <StructureSection load='7qrv' size='340' side='right'caption='[[7qrv]]' scene=''> | + | <StructureSection load='7qrv' size='340' side='right'caption='[[7qrv]], [[Resolution|resolution]] 1.45Å' 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=7QRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qrv]] is a 4 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=7QRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRV 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=7qrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qrv OCA], [https://pdbe.org/7qrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qrv RCSB], [https://www.ebi.ac.uk/pdbsum/7qrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qrv 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]] 1.45Å</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=7qrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qrv OCA], [https://pdbe.org/7qrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qrv RCSB], [https://www.ebi.ac.uk/pdbsum/7qrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qrv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/TRIM2_HUMAN TRIM2_HUMAN] Charcot-Marie-Tooth disease type 2R. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRIM2_HUMAN TRIM2_HUMAN] UBE2D1-dependent E3 ubiquitin-protein ligase that mediates the ubiquitination of NEFL and of phosphorylated BCL2L11. Plays a neuroprotective function. May play a role in neuronal rapid ischemic tolerance.[UniProtKB:Q9ESN6] | ||
| + | <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 7qrv" style="background-color:#fffaf0;"></div> | ||
| + | == 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]] | ||
[[Category: Zhubi R]] | [[Category: Zhubi R]] | ||
Current revision
Crystal structure of NHL domain of TRIM2 (full C-terminal)
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