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1r4x

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Revision as of 08:08, 28 February 2018

Crystal Structure Analys of the Gamma-COPI Appendage domain

Structural highlights

1r4x is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1pzd, 1b9k, 1e42
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COPG1_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. 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).^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the beta-, gamma-, delta- and zeta-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the alpha-, beta'- and epsilon-COP subunits. Here, we present the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex.

Gamma-COP appendage domain - structure and function.,Watson PJ, Frigerio G, Collins BM, Duden R, Owen DJ Traffic. 2004 Feb;5(2):79-88. PMID:14690497^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang YN, Wang H, Yamaguchi H, Lee HJ, Lee HH, Hung MC. COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport. Biochem Biophys Res Commun. 2010 Sep 3;399(4):498-504. doi:, 10.1016/j.bbrc.2010.07.096. Epub 2010 Jul 30. PMID:20674546 doi:http://dx.doi.org/10.1016/j.bbrc.2010.07.096
↑ Watson PJ, Frigerio G, Collins BM, Duden R, Owen DJ. Gamma-COP appendage domain - structure and function. Traffic. 2004 Feb;5(2):79-88. PMID:14690497

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r4x"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analys of the Gamma-COPI Appendage domain==
 <StructureSection load='1r4x' size='340' side='right' caption='[[1r4x]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pzd|1pzd]], [[1b9k|1b9k]], [[1e42|1e42]]</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=1r4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4x OCA], [http://pdbe.org/1r4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4x RCSB], [http://www.ebi.ac.uk/pdbsum/1r4x PDBsum]</span></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=1r4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4x OCA], [http://pdbe.org/1r4x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4x RCSB], [http://www.ebi.ac.uk/pdbsum/1r4x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4x ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r4x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r4x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1r4x

From Proteopedia

Revision as of 08:08, 28 February 2018

Crystal Structure Analys of the Gamma-COPI Appendage domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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