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| | <StructureSection load='5gw1' size='340' side='right'caption='[[5gw1]], [[Resolution|resolution]] 3.35Å' scene=''> | | <StructureSection load='5gw1' size='340' side='right'caption='[[5gw1]], [[Resolution|resolution]] 3.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gw1]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GW1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GW1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gw1]] is a 8 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=5GW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GW1 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gw0|5gw0]], [[5gw8|5gw8]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5gw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw1 OCA], [http://pdbe.org/5gw1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gw1 RCSB], [http://www.ebi.ac.uk/pdbsum/5gw1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw1 ProSAT]</span></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=5gw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gw1 OCA], [https://pdbe.org/5gw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gw1 RCSB], [https://www.ebi.ac.uk/pdbsum/5gw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gw1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, J]] | + | [[Category: Liu J]] |
| - | [[Category: Xu, J]] | + | [[Category: Xu J]] |
| - | [[Category: Endosome sorting]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Px domain]]
| + | |
| - | [[Category: Sortin nexin]]
| + | |
| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hanson BJ, Hong W. Evidence for a role of SNX16 in regulating traffic between the early and later endosomal compartments. J Biol Chem. 2003 Sep 5;278(36):34617-30. Epub 2003 Jun 17. PMID:12813048 doi:http://dx.doi.org/10.1074/jbc.M300143200
- ↑ Le Blanc I, Luyet PP, Pons V, Ferguson C, Emans N, Petiot A, Mayran N, Demaurex N, Faure J, Sadoul R, Parton RG, Gruenberg J. Endosome-to-cytosol transport of viral nucleocapsids. Nat Cell Biol. 2005 Jul;7(7):653-64. Epub 2005 Jun 12. PMID:15951806 doi:http://dx.doi.org/10.1038/ncb1269
- ↑ Xu J, Zhang L, Ye Y, Shan Y, Wan C, Wang J, Pei D, Shu X, Liu J. SNX16 Regulates the Recycling of E-Cadherin through a Unique Mechanism of Coordinated Membrane and Cargo Binding. Structure. 2017 Aug 1;25(8):1251-1263.e5. doi: 10.1016/j.str.2017.06.015. Epub, 2017 Jul 14. PMID:28712807 doi:http://dx.doi.org/10.1016/j.str.2017.06.015
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