8d41
From Proteopedia
(Difference between revisions)
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==Crystal structure of the human COPB2 WD-domain in complex with OICR-6254== | ==Crystal structure of the human COPB2 WD-domain in complex with OICR-6254== | ||
| - | <StructureSection load='8d41' size='340' side='right'caption='[[8d41]]' scene=''> | + | <StructureSection load='8d41' size='340' side='right'caption='[[8d41]], [[Resolution|resolution]] 2.00Å' 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=8D41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D41 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[8d41]] 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=8D41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D41 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=8d41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d41 OCA], [https://pdbe.org/8d41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d41 RCSB], [https://www.ebi.ac.uk/pdbsum/8d41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d41 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=Q93:(1R,2R,3S,4S)-3-[4-(4-fluorophenyl)piperazine-1-carbonyl]bicyclo[2.2.1]heptane-2-carboxylic+acid'>Q93</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=8d41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d41 OCA], [https://pdbe.org/8d41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d41 RCSB], [https://www.ebi.ac.uk/pdbsum/8d41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d41 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/COPB2_HUMAN COPB2_HUMAN]] Autosomal recessive primary microcephaly. The disease may be caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/COPB2_HUMAN COPB2_HUMAN]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner (By similarity). | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arrowsmith CH]] | [[Category: Arrowsmith CH]] | ||
Revision as of 06:51, 8 September 2022
Crystal structure of the human COPB2 WD-domain in complex with OICR-6254
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Categories: Homo sapiens | Large Structures | Arrowsmith CH | Dong A | Edwards AM | Halabelian L | Hutchinson A | Loppnau P | Saraon P | Seitova A | Zeng H
