View source for 7jhx


==Crystal structure of hEPG5 LIR/GABARAPL1 complex==
<StructureSection load='7jhx' size='340' side='right'caption='[[7jhx]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jhx]] 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=7JHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JHX 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]] 1.91&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=7jhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jhx OCA], [https://pdbe.org/7jhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jhx RCSB], [https://www.ebi.ac.uk/pdbsum/7jhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jhx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GBRL1_HUMAN GBRL1_HUMAN] Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor. Involved in formation of autophagosomal vacuoles.<ref>PMID:16431922</ref> <ref>PMID:20404487</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pivotal to the maintenance of cellular homeostasis, macroautophagy (hereafter autophagy) is an evolutionarily conserved degradation system that involves sequestration of cytoplasmic material into the double-membrane autophagosome and targeting of this transport vesicle to the lysosome/late endosome for degradation. EPG5 is a large-sized metazoan protein proposed to serve as a tethering factor to enforce autophagosome-lysosome/late endosome fusion specificity, and its deficiency causes a severe multisystem disorder known as Vici syndrome. Here, we show that human EPG5 (hEPG5) adopts an extended "shepherd's staff" architecture. We find that hEPG5 binds preferentially to members of the GABARAP subfamily of human ATG8 proteins critical to autophagosome-lysosome fusion. The hEPG5-GABARAPs interaction, which is mediated by tandem LIR motifs that exhibit differential affinities, is required for hEPG5 recruitment to mitochondria during PINK1/Parkin-dependent mitophagy. Lastly, we find that the Vici syndrome mutation Gln336Arg does not affect the hEPG5's overall stability nor its ability to engage in interaction with the GABARAPs. Collectively, results from our studies reveal new insights into how hEPG5 recognizes mature autophagosome and establish a platform for examining the molecular effects of Vici syndrome disease mutations on hEPG5.

Insights on autophagosome-lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5.,Nam SE, Cheung YWS, Nguyen TN, Gong M, Chan S, Lazarou M, Yip CK Commun Biol. 2021 Mar 5;4(1):291. doi: 10.1038/s42003-021-01830-x. PMID:33674710<ref>PMID:33674710</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jhx" style="background-color:#fffaf0;"></div>

==See Also==
*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cheung YWS]]
[[Category: Yip CK]]