5f0m: Difference between revisions

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-'''Unreleased structure'''
-The entry 5f0m is ON HOLD  until Paper Publication
+==Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1 (SeMet labeled)==
+<StructureSection load='5f0m' size='340' side='right'caption='[[5f0m]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5f0m]] is a 4 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=5F0M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F0M 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]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5f0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f0m OCA], [https://pdbe.org/5f0m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f0m RCSB], [https://www.ebi.ac.uk/pdbsum/5f0m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f0m ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/VPS35_HUMAN VPS35_HUMAN] Defects in VPS35 are the cause of Parkinson disease type 17 (PARK17) [MIM:[https://omim.org/entry/614203 614203]. PARK17 is an autosomal dominant, adult-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.<ref>PMID:21763482</ref> <ref>PMID:21763483</ref> <ref>PMID:22517097</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/VPS35_HUMAN VPS35_HUMAN] Essential component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network. Also required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA).<ref>PMID:15247922</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Retromer is a multi-protein complex that recycles transmembrane cargo from endosomes to the trans-Golgi network and the plasma membrane. Defects in retromer impair various cellular processes and underlie some forms of Alzheimer's disease and Parkinson's disease. Although retromer was discovered over 15 years ago, the mechanisms for cargo recognition and recruitment to endosomes have remained elusive. Here, we present an X-ray crystallographic analysis of a four-component complex comprising the VPS26 and VPS35 subunits of retromer, the sorting nexin SNX3, and a recycling signal from the divalent cation transporter DMT1-II. This analysis identifies a binding site for canonical recycling signals at the interface between VPS26 and SNX3. In addition, the structure highlights a network of cooperative interactions among the VPS subunits, SNX3, and cargo that couple signal-recognition to membrane recruitment.
-Authors: Lucas, M., Gershlick, D., Vidaurrazaga, A., Rojas, A.L., Bonifacino, J.S., Hierro, A.
+Structural Mechanism for Cargo Recognition by the Retromer Complex.,Lucas M, Gershlick DC, Vidaurrazaga A, Rojas AL, Bonifacino JS, Hierro A Cell. 2016 Dec 1;167(6):1623-1635.e14. doi: 10.1016/j.cell.2016.10.056. Epub 2016, Nov 23. PMID:27889239<ref>PMID:27889239</ref>
-Description: Endosomal sorting complex
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Bonifacino, J.S]]
+<div class="pdbe-citations 5f0m" style="background-color:#fffaf0;"></div>
-[[Category: Hierro, A]]
-[[Category: Gershlick, D]]
+==See Also==
-[[Category: Lucas, M]]
+*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
-[[Category: Vidaurrazaga, A]]
+*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
-[[Category: Rojas, A.L]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Bonifacino JS]]
+[[Category: Gershlick D]]
+[[Category: Hierro A]]
+[[Category: Lucas M]]
+[[Category: Rojas AL]]
+[[Category: Vidaurrazaga A]]