View source for 4aiw


==GAPR-1 with bound inositol hexakisphosphate==
<StructureSection load='4aiw' size='340' side='right'caption='[[4aiw]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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='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>
== Function ==
[https://www.uniprot.org/uniprot/GAPR1_HUMAN GAPR1_HUMAN] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:22560898</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aiw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Siderocalin 3D structures|Siderocalin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Gros P]]
[[Category: Helms JB]]
[[Category: Schouten A]]