3g2t
From Proteopedia
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| - | {{STRUCTURE_3g2t| PDB=3g2t | SCENE= }} | ||
| - | ===VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide=== | ||
| - | {{ABSTRACT_PUBMED_20015111}} | ||
| - | == | + | ==VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide== |
| - | [[http://www.uniprot.org/uniprot/GGA1_HUMAN GGA1_HUMAN | + | <StructureSection load='3g2t' size='340' side='right'caption='[[3g2t]], [[Resolution|resolution]] 2.00Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3g2t]] is a 4 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=3G2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G2T 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]] 2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=3g2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2t OCA], [https://pdbe.org/3g2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g2t RCSB], [https://www.ebi.ac.uk/pdbsum/3g2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g2t ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GGA1_HUMAN GGA1_HUMAN] Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif.<ref>PMID:11301005</ref> | ||
| + | == 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/g2/3g2t_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=3g2t ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cytosolic adaptors GGA1-3 mediate sorting of transmembrane proteins displaying a C-terminal acidic dileucine motif (DXXLL) in their cytosolic domain. GGA1 and GGA3 contain similar but intrinsic motifs that are believed to serve as autoinhibitory sites activated by the phosphorylation of a serine positioned three residues upstream of the DXXLL motif. In the present study, we have subjected the widely acknowledged concept of GGA1 autoinhibition to a thorough structural and functional examination. We find that (i) the intrinsic motif of GGA1 is inactive, (ii) only C-terminal DXXLL motifs constitute active GGA binding sites, (iii) while aspartates and phosphorylated serines one or two positions upstream of the DXXLL motif increase GGA1 binding, phosphoserines further upstream have little or no influence and (iv) phosphorylation of GGA1 does not affect its conformation or binding to Sortilin and SorLA. Taken together, our findings seem to refute the functional significance of GGA autoinhibition in particular and of intrinsic GGA binding motifs in general. | ||
| - | + | GGA Autoinhibition Revisited.,Cramer JF, Gustafsen C, Behrens MA, Oliveira CL, Pedersen JS, Madsen P, Petersen CM, Thirup SS Traffic. 2010 Feb;11(2):259-73. Epub 2009 Nov 10. PMID:20015111<ref>PMID:20015111</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 3g2t" style="background-color:#fffaf0;"></div> |
| - | [[Category: Behrens | + | == References == |
| - | [[Category: Cramer | + | <references/> |
| - | [[Category: Gustafsen | + | __TOC__ |
| - | [[Category: Madsen | + | </StructureSection> |
| - | [[Category: Oliveira | + | [[Category: Homo sapiens]] |
| - | [[Category: Pedersen | + | [[Category: Large Structures]] |
| - | [[Category: Petersen | + | [[Category: Behrens MA]] |
| - | [[Category: Thirup | + | [[Category: Cramer JF]] |
| - | + | [[Category: Gustafsen C]] | |
| - | + | [[Category: Madsen P]] | |
| - | + | [[Category: Oliveira CLP]] | |
| - | + | [[Category: Pedersen JS]] | |
| - | + | [[Category: Petersen CM]] | |
| + | [[Category: Thirup SS]] | ||
Current revision
VHS Domain of human GGA1 complexed with SorLA C-terminal Phosphopeptide
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