View source for 5gw0


==Crystal structure of SNX16 PX-Coiled coil==
<StructureSection load='5gw0' size='340' side='right'caption='[[5gw0]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gw0]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GW0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GW0 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gw1|5gw1]], [[5gw8|5gw8]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw0 OCA], [http://pdbe.org/5gw0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gw0 RCSB], [http://www.ebi.ac.uk/pdbsum/5gw0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw0 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SNX16_HUMAN SNX16_HUMAN]] May be involved in several stages of intracellular trafficking. Plays a role in protein transport from early to late endosomes. Plays a role in protein transport to the lysosome. Promotes degradation of EGFR after EGF signaling. Plays a role in intracellular transport of vesicular stomatitis virus nucleocapsids from the endosome to the cytoplasm.<ref>PMID:12813048</ref> <ref>PMID:15951806</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
E-Cadherin is a major component of adherens junctions on cell surfaces. SNX16 is a unique member of sorting nexins that contains a coiled-coil (CC) domain downstream of the PX domain. We report here that SNX16 regulates the recycling trafficking of E-cadherin. We solved the crystal structure of PX-CC unit of SNX16 and revealed a unique shear shaped homodimer. We identified a novel PI3P binding pocket in SNX16 that consists of both the PX and the CC domains. Surprisingly, we showed that the PPII/alpha2 loop, which is generally regarded as a membrane insertion loop in PX family proteins, is involved in the E-cadherin binding with SNX16. We then proposed a multivalent membrane binding model for SNX16. Our study postulates a new mechanism for coordinated membrane binding and cargo binding for SNX family proteins in general, and provide novel insights into recycling trafficking of E-cadherin.

SNX16 Regulates the Recycling of E-Cadherin through a Unique Mechanism of Coordinated Membrane and Cargo Binding.,Xu J, Zhang L, Ye Y, Shan Y, Wan C, Wang J, Pei D, Shu X, Liu J Structure. 2017 Aug 1;25(8):1251-1263.e5. doi: 10.1016/j.str.2017.06.015. Epub, 2017 Jul 14. PMID:28712807<ref>PMID:28712807</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gw0" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Liu, J]]
[[Category: Xu, J]]
[[Category: Endosome sorting]]
[[Category: Protein transport]]
[[Category: Px domain]]
[[Category: Sorting nexin]]