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3g2s

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Revision as of 10:35, 9 September 2020

VHS Domain of human GGA1 complexed with SorLA C-terminal Peptide

Structural highlights

3g2s is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3g2t, 3g2u, 3g2v, 3g2w
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [SORL_HUMAN] Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction.

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

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^[2]

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

References

↑ Puertollano R, Randazzo PA, Presley JF, Hartnell LM, Bonifacino JS. The GGAs promote ARF-dependent recruitment of clathrin to the TGN. Cell. 2001 Apr 6;105(1):93-102. PMID:11301005
↑ Cramer JF, Gustafsen C, Behrens MA, Oliveira CL, Pedersen JS, Madsen P, Petersen CM, Thirup SS. GGA Autoinhibition Revisited. Traffic. 2010 Feb;11(2):259-73. Epub 2009 Nov 10. PMID:20015111 doi:http://dx.doi.org/TRA1017

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/3g2s"

@@ Line 1: / Line 1: @@
 ==VHS Domain of human GGA1 complexed with SorLA C-terminal Peptide==
-<StructureSection load='3g2s' size='340' side='right' caption='[[3g2s]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='3g2s' size='340' side='right'caption='[[3g2s]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3g2s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G2S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G2S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3g2s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G2S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3G2S FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g2t|3g2t]], [[3g2u|3g2u]], [[3g2v|3g2v]], [[3g2w|3g2w]]</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=3g2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2s OCA], [http://pdbe.org/3g2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g2s RCSB], [http://www.ebi.ac.uk/pdbsum/3g2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g2s ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3g2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2s OCA], [http://pdbe.org/3g2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g2s RCSB], [http://www.ebi.ac.uk/pdbsum/3g2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g2s ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Behrens, M A]]
 [[Category: Cramer, J F]]

3g2s

From Proteopedia

Revision as of 10:35, 9 September 2020

VHS Domain of human GGA1 complexed with SorLA C-terminal Peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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