4pzg

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==Crystal structure of human sorting nexin 10 (SNX10)==
==Crystal structure of human sorting nexin 10 (SNX10)==
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<StructureSection load='4pzg' size='340' side='right' caption='[[4pzg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='4pzg' size='340' side='right'caption='[[4pzg]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4pzg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PZG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PZG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4pzg]] is a 2 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=4PZG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PZG FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4on3|4on3]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pzg RCSB], [http://www.ebi.ac.uk/pdbsum/4pzg PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pzg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pzg OCA], [https://pdbe.org/4pzg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pzg RCSB], [https://www.ebi.ac.uk/pdbsum/4pzg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pzg ProSAT]</span></td></tr>
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<table>
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</table>
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== Disease ==
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<div style="background-color:#fffaf0;">
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[[http://www.uniprot.org/uniprot/SNX10_HUMAN SNX10_HUMAN]] Autosomal recessive malignant osteopetrosis. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:22499339</ref> <ref>PMID:23123320</ref> <ref>PMID:23280965</ref>
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== Publication Abstract from PubMed ==
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== Function ==
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Sorting nexin 10 (SNX10), the unique member of the SNX family having vacuolation activity in cells, was shown to be involved in the development of autosomal recessive osteopetrosis (ARO) in recent genetic studies. However, the molecular mechanism of the disease-related mutations affecting the biological function of SNX10 is unclear. Here, we report the crystal structure of human SNX10 to 2.6A resolution. The structure reveals that SNX10 contains the extended phox-homology domain we previously proposed. Our study provides the structural details of those disease-related mutations. Combined with the vacuolation study of those mutations, we found that Tyr32 and Arg51 are important for the protein stability and both play a critical role in vacuolation activity, while Arg16Leu may affect the function of SNX10 in osteoclast through protein-protein interactions. Proteins 2014; 82:3483-3489. (c) 2014 Wiley Periodicals, Inc.
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[[http://www.uniprot.org/uniprot/SNX10_HUMAN SNX10_HUMAN]] Probable phosphoinositide-binding protein involved in protein sorting and membrane trafficking in endosomes. Plays a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. Required for the localization to the cilium of V-ATPase subunit ATP6V1D and ATP6V0D1, and RAB8A. Involved in osteoclast differentiation and therefore bone resorption.<ref>PMID:17012226</ref> <ref>PMID:21844891</ref> <ref>PMID:22499339</ref>
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Structure of human SNX10 reveals insights into its role in human autosomal recessive osteopetrosis.,Xu T, Xu J, Ye Y, Wang Q, Shu X, Pei D, Liu J Proteins. 2014 Dec;82(12):3483-9. doi: 10.1002/prot.24689. Epub 2014 Oct 1. PMID:25212774<ref>PMID:25212774</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pzg" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Liu, J.]]
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[[Category: Homo sapiens]]
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[[Category: Wang, Q.]]
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[[Category: Large Structures]]
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[[Category: Xu, J.]]
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[[Category: Liu J]]
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[[Category: Xu, T.]]
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[[Category: Wang Q]]
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[[Category: Phox-homology domain]]
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[[Category: Xu J]]
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[[Category: Protein transport]]
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[[Category: Xu T]]
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[[Category: Sorting nexin]]
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Current revision

Crystal structure of human sorting nexin 10 (SNX10)

PDB ID 4pzg

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