5gw1

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of SNX16 PX-Coiled coil in space group P212121

Structural highlights

5gw1 is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.35Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gw1"

Categories: Homo sapiens | Large Structures | Liu J | Xu J

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5gw1 is ON HOLD  until Paper Publication
+==Crystal structure of SNX16 PX-Coiled coil in space group P212121==
+<StructureSection load='5gw1' size='340' side='right'caption='[[5gw1]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</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'>[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>
+== Function ==
+[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;">
+== 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.
-Authors: Xu, J., Liu, J.
+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>
-Description: Crystal structure of SNX16 PX-Coiled coil in space group P212121
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Liu, J]]
+<div class="pdbe-citations 5gw1" style="background-color:#fffaf0;"></div>
-[[Category: Xu, J]]
+==See Also==
+*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Liu J]]
+[[Category: Xu J]]

5gw1

From Proteopedia

Current revision

Crystal structure of SNX16 PX-Coiled coil in space group P212121

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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