6e7o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of deglycosylated human EPDR1== | |
| + | <StructureSection load='6e7o' size='340' side='right' caption='[[6e7o]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6e7o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E7O FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6e8n|6e8n]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EPDR1, MERP1, UCC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e7o OCA], [http://pdbe.org/6e7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e7o RCSB], [http://www.ebi.ac.uk/pdbsum/6e7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e7o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | EPDR1, a member of the ependymin-related protein family, is a relatively uncharacterized protein found in the lysosomes and secretomes of most vertebrates. Despite having roles in human disease and health, the molecular functions of EPDR1 remain unknown. Here, we present crystal structures of human EPDR1 and reveal that the protein adopts a fold previously seen only in bacterial proteins related to the LolA lipoprotein transporter. EPDR1 forms a homodimer with an overall shape resembling a half-shell with two non-overlapping hydrophobic grooves on the flat side of the hemisphere. EPDR1 can interact with membranes that contain negatively charged lipids, including BMP and GM1, and we suggest that EPDR1 may function as a lysosomal activator protein or a lipid transporter. A phylogenetic analysis reveals that the fold is more widely distributed than previously suspected, with representatives identified in all branches of cellular life. | ||
| - | + | Crystal structures of human lysosomal EPDR1 reveal homology with the superfamily of bacterial lipoprotein transporters.,Wei Y, Xiong ZJ, Li J, Zou C, Cairo CW, Klassen JS, Prive GG Commun Biol. 2019 Feb 5;2:52. doi: 10.1038/s42003-018-0262-9. eCollection 2019. PMID:30729188<ref>PMID:30729188</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Prive, G]] | + | <div class="pdbe-citations 6e7o" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Prive, G G]] | ||
[[Category: Wei, Y]] | [[Category: Wei, Y]] | ||
| + | [[Category: Lipid binding]] | ||
| + | [[Category: Lipid binding protein]] | ||
| + | [[Category: Lola fold]] | ||
| + | [[Category: Lysosomal protein]] | ||
| + | [[Category: Secreted protein]] | ||
Revision as of 08:37, 21 February 2019
Crystal structure of deglycosylated human EPDR1
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