View source for 7qrw


==Crystal structure of NHL domain of TRIM3==
<StructureSection load='7qrw' size='340' side='right'caption='[[7qrw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qrw]] is a 1 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=7QRW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QRW 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]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7qrw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qrw OCA], [https://pdbe.org/7qrw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qrw RCSB], [https://www.ebi.ac.uk/pdbsum/7qrw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qrw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRIM3_HUMAN TRIM3_HUMAN] Probably involved in vesicular trafficking via its association with the CART complex (PubMed:15772161). The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Positively regulates motility of microtubule-dependent motor protein KIF21B (By similarity).[UniProtKB:Q9R1R2]<ref>PMID:15772161</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qrw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chaikuad A]]
[[Category: Knapp S]]