View source for 6edx


==Crystal Structure of SGK3 PX domain==
<StructureSection load='6edx' size='340' side='right'caption='[[6edx]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6edx]] is a 1 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=6EDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EDX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGK3, CISK, SGKL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=6edx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6edx OCA], [http://pdbe.org/6edx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6edx RCSB], [http://www.ebi.ac.uk/pdbsum/6edx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6edx ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SGK3_HUMAN SGK3_HUMAN]] Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, proliferation, survival and migration. Up-regulates Na(+) channels: SCNN1A/ENAC and SCN5A, K(+) channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger: SLC9A3/NHE3, and the Na(+)/K(+) ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes.<ref>PMID:12054501</ref> <ref>PMID:12397388</ref> <ref>PMID:12590200</ref> <ref>PMID:12632189</ref> <ref>PMID:12634932</ref> <ref>PMID:12650886</ref> <ref>PMID:12911626</ref> <ref>PMID:14706641</ref> <ref>PMID:15040001</ref> <ref>PMID:15044175</ref> <ref>PMID:15319523</ref> <ref>PMID:15496163</ref> <ref>PMID:15737648</ref> <ref>PMID:15845389</ref> <ref>PMID:16036218</ref> <ref>PMID:16888620</ref> <ref>PMID:17167223</ref> <ref>PMID:18005662</ref> <ref>PMID:19293151</ref> <ref>PMID:20511718</ref> <ref>PMID:21865597</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family.

Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.,Chandra M, Chin YK, Mas C, Feathers JR, Paul B, Datta S, Chen KE, Jia X, Yang Z, Norwood SJ, Mohanty B, Bugarcic A, Teasdale RD, Henne WM, Mobli M, Collins BM Nat Commun. 2019 Apr 4;10(1):1528. doi: 10.1038/s41467-019-09355-y. PMID:30948714<ref>PMID:30948714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6edx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Chandra, M]]
[[Category: Collins, B M]]
[[Category: Endosome]]
[[Category: Px domain]]
[[Category: Sorting nexin]]
[[Category: Trafficking]]
[[Category: Transferase]]