View source for 9jxk


==Cryo-EM structure of human XPR1 in a closed state at the intracellular gate and an open state at the extracellular gate, obtained through local refinement==
<StructureSection load='9jxk' size='340' side='right'caption='[[9jxk]], [[Resolution|resolution]] 3.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9jxk]] 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=9JXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9JXK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=9jxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9jxk OCA], [https://pdbe.org/9jxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9jxk RCSB], [https://www.ebi.ac.uk/pdbsum/9jxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9jxk ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Bilateral striopallidodentate calcinosis. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity) (PubMed:23791524, PubMed:25938945, PubMed:31043717). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106).[UniProtKB:Q9Z0U0]<ref>PMID:23791524</ref> <ref>PMID:25938945</ref> <ref>PMID:27080106</ref> <ref>PMID:31043717</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bai Z]]
[[Category: Corry B]]
[[Category: Gu C]]
[[Category: Han Y]]
[[Category: Jessen H]]
[[Category: Jin R]]
[[Category: Lei M]]
[[Category: Shears S]]
[[Category: Sun Y]]
[[Category: Wallis C]]
[[Category: Wang H]]
[[Category: Wang X]]
[[Category: Zhang Y]]