6pbg

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Current revision (07:26, 11 October 2023) (edit) (undo)
 
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<StructureSection load='6pbg' size='340' side='right'caption='[[6pbg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='6pbg' size='340' side='right'caption='[[6pbg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pbg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PBG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pbg]] 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=6PBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PBG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
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<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=6pbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pbg OCA], [http://pdbe.org/6pbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pbg RCSB], [http://www.ebi.ac.uk/pdbsum/6pbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pbg ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pbg OCA], [https://pdbe.org/6pbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pbg RCSB], [https://www.ebi.ac.uk/pdbsum/6pbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pbg ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/COPA_HUMAN COPA_HUMAN]] Autoimmune interstitial lung disease-arthritis syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/COPA_HUMAN COPA_HUMAN] Autoimmune interstitial lung disease-arthritis syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/COPA_HUMAN COPA_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). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.
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[https://www.uniprot.org/uniprot/COPA_HUMAN COPA_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). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Dong, A]]
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[[Category: Dong A]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Halabelian, L]]
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[[Category: Halabelian L]]
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[[Category: Hutchinson, A]]
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[[Category: Hutchinson A]]
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[[Category: Loppnau, P]]
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[[Category: Loppnau P]]
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[[Category: Structural genomic]]
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[[Category: Seitova A]]
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[[Category: Seitova, A]]
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[[Category: Zeng H]]
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[[Category: Zeng, H]]
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[[Category: Coatomer subunit alpha]]
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[[Category: Copa]]
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[[Category: Protein transport]]
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[[Category: Sgc]]
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[[Category: Wd-repeat]]
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Current revision

Crystal structure of WD-repeat domain of human coatomer subunit Alpha (COPA)

PDB ID 6pbg

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