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| <StructureSection load='4aiw' size='340' side='right'caption='[[4aiw]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4aiw' size='340' side='right'caption='[[4aiw]], [[Resolution|resolution]] 1.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4aiw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4aiw]] 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=4AIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIW FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1smb|1smb]]</div></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=4aiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aiw OCA], [https://pdbe.org/4aiw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aiw RCSB], [https://www.ebi.ac.uk/pdbsum/4aiw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aiw ProSAT]</span></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=4aiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aiw OCA], [https://pdbe.org/4aiw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aiw RCSB], [https://www.ebi.ac.uk/pdbsum/4aiw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aiw ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/GAPR1_HUMAN GAPR1_HUMAN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Gros, P]] | + | [[Category: Gros P]] |
- | [[Category: Helms, J B]] | + | [[Category: Helms JB]] |
- | [[Category: Schouten, A]] | + | [[Category: Schouten A]] |
- | [[Category: Golgi apparatus]]
| + | |
- | [[Category: Lipid binding protein]]
| + | |
- | [[Category: Lipid-binding protein]]
| + | |
- | [[Category: Myristate]]
| + | |
| Structural highlights
Function
GAPR1_HUMAN
Publication Abstract from PubMed
Golgi-Associated Plant Pathogenesis-Related protein 1 (GAPR-1) is a mammalian protein that belongs to the superfamily of plant pathogenesis related proteins group 1 (PR-1). GAPR-1 is a peripheral membrane-binding protein that strongly associates with lipid-enriched microdomains at the cytosolic leaflet of Golgi membranes. Little is known about the mechanism of GAPR-1 interaction with membranes. We previously suggested that dimerization plays a role in the function of GAPR-1 and here we report that phytic acid (inositol hexakisphosphate) induces dimerization of GAPR-1 in solution. Elucidation of the crystal structure of GAPR-1 in the presence of phytic acid revealed that the GAPR-1 dimer differs from the previously published GAPR-1 dimer structure. In this structure, one of the monomeric subunits of the crystallographic dimer is rotated by 28.5 degrees . To study the GAPR-1 dimerization properties, we investigated the interaction with liposomes in a light scattering assay and by flow cytometry. In the presence of negatively charged lipids, GAPR-1 caused a rapid and stable tethering of liposomes. [D81K]GAPR-1, a mutant predicted to stabilize the IP6-induced dimer conformation, also caused tethering of liposomes. [A68K]GAPR-1 however, a mutant predicted to stabilize the non-rotated dimer conformation, is capable of binding to liposomes but did not cause liposome tethering. Our combined data suggest that the charge properties of the lipid bilayer can regulate GAPR-1 dynamics as a potential mechanism to modulate GAPR-1 function.
Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization.,van Galen J, Olrichs NK, Schouten A, Serrano RL, Nolte-'t Hoen EN, Eerland R, Kaloyanova D, Gros P, Helms JB Biochim Biophys Acta. 2012 Sep;1818(9):2175-83. Epub 2012 Apr 26. PMID:22560898[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ van Galen J, Olrichs NK, Schouten A, Serrano RL, Nolte-'t Hoen EN, Eerland R, Kaloyanova D, Gros P, Helms JB. Interaction of GAPR-1 with lipid bilayers is regulated by alternative homodimerization. Biochim Biophys Acta. 2012 Sep;1818(9):2175-83. Epub 2012 Apr 26. PMID:22560898 doi:10.1016/j.bbamem.2012.04.016
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