1pzd
From Proteopedia
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| - | [[Image:1pzd.png|left|200px]] | ||
| - | + | ==Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.== | |
| - | + | <StructureSection load='1pzd' size='340' side='right'caption='[[1pzd]], [[Resolution|resolution]] 2.31Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1pzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PZD 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]] 2.31Å</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=1pzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzd OCA], [https://pdbe.org/1pzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pzd RCSB], [https://www.ebi.ac.uk/pdbsum/1pzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pzd ProSAT]</span></td></tr> |
| - | [[1pzd]] is a 1 chain structure with sequence from [ | + | </table> |
| - | + | == Function == | |
| - | == | + | [https://www.uniprot.org/uniprot/COPG1_BOVIN COPG1_BOVIN] 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. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity). |
| - | < | + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pz/1pzd_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pzd ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Cerione RA]] |
| - | [[Category: | + | [[Category: Collins RN]] |
| - | [[Category: | + | [[Category: Hoffman GR]] |
| - | [[Category: | + | [[Category: Rahl PB]] |
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Current revision
Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.
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