2mxc: Difference between revisions
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<StructureSection load='2mxc' size='340' side='right' caption='[[2mxc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2mxc' size='340' side='right' caption='[[2mxc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mxc]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MXC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MXC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2mxc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MXC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MXC FirstGlance]. <br> | ||
</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=2mxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxc OCA], [http://pdbe.org/2mxc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mxc RCSB], [http://www.ebi.ac.uk/pdbsum/2mxc PDBsum]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNX3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2mxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mxc OCA], [http://pdbe.org/2mxc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mxc RCSB], [http://www.ebi.ac.uk/pdbsum/2mxc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mxc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SNX3_HUMAN SNX3_HUMAN]] Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in protein transport between cellular compartments. Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation.<ref>PMID:11433298</ref> <ref>PMID:18767904</ref> | [[http://www.uniprot.org/uniprot/SNX3_HUMAN SNX3_HUMAN]] Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Plays a role in protein transport between cellular compartments. Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G (By similarity). Not involved in EGFR degradation.<ref>PMID:11433298</ref> <ref>PMID:18767904</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sorting nexins anchor trafficking machines to membranes by binding phospholipids. The paradigm of the superfamily is sorting nexin 3 (SNX3), which localizes to early endosomes by recognizing phosphatidylinositol 3-phosphate (PI3P) to initiate retromer-mediated segregation of cargoes to the trans-Golgi network (TGN). Here we report the solution structure of full length human SNX3, and show that PI3P recognition is accompanied by bilayer insertion of a proximal loop in its extended Phox homology (PX) domain. Phosphoinositide (PIP) binding is completely blocked by cancer-linked phosphorylation of a conserved serine beside the stereospecific PI3P pocket. This "PIP-stop" releases endosomal SNX3 to the cytosol, and reveals how protein kinases control membrane assemblies. It constitutes a widespread regulatory element found across the PX superfamily and throughout evolution including of fungi and plants. This illuminates the mechanism of a biological switch whereby structured PIP sites are phosphorylated to liberate protein machines from organelle surfaces. | |||
Phosphorylation of conserved phosphoinositide binding pocket regulates sorting nexin membrane targeting.,Lenoir M, Ustunel C, Rajesh S, Kaur J, Moreau D, Gruenberg J, Overduin M Nat Commun. 2018 Mar 8;9(1):993. doi: 10.1038/s41467-018-03370-1. PMID:29520003<ref>PMID:29520003</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mxc" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Sorting nexin|Sorting nexin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | |||
[[Category: Gruenberg, J J.G]] | [[Category: Gruenberg, J J.G]] | ||
[[Category: Kaur, J J.K]] | [[Category: Kaur, J J.K]] | ||