5f2u
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5f2u is ON HOLD Authors: Fansa, E.K., Isamil, S., Wittinghofer, A. Description: Structure of Fully modified farnesylated INPP5E Peptide in complex ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Fully modified farnesylated INPP5E Peptide in complex with PDE6D== | |
| + | <StructureSection load='5f2u' size='340' side='right'caption='[[5f2u]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5f2u]] 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=5F2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F2U 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]] 1.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene>, <scene name='pdbligand=FAR:FARNESYL'>FAR</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=5f2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2u OCA], [https://pdbe.org/5f2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f2u RCSB], [https://www.ebi.ac.uk/pdbsum/5f2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f2u ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PDE6D_HUMAN PDE6D_HUMAN] Acts as a GTP specific dissociation inhibitor (GDI). Increases the affinity of ARL3 for GTP by several orders of magnitude and does so by decreasing the nucleotide dissociation rate. Stabilizes Arl3-GTP by decreasing the nucleotide dissociation (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The phosphodiesterase 6 delta subunit (PDE6delta) shuttles several farnesylated cargos between membranes. The cargo sorting mechanism between cilia and other compartments is not understood. Here we show using the inositol polyphosphate 5'-phosphatase E (INPP5E) and the GTP-binding protein (Rheb) that cargo sorting depends on the affinity towards PDE6delta and the specificity of cargo release. High-affinity cargo is exclusively released by the ciliary transport regulator Arl3, while low-affinity cargo is released by Arl3 and its non-ciliary homologue Arl2. Structures of PDE6delta/cargo complexes reveal the molecular basis of the sorting signal which depends on the residues at the -1 and -3 positions relative to farnesylated cysteine. Structure-guided mutation allows the generation of a low-affinity INPP5E mutant which loses exclusive ciliary localization. We postulate that the affinity to PDE6delta and the release by Arl2/3 in addition to a retention signal are the determinants for cargo sorting and enrichment at its destination. | ||
| - | + | PDE6delta-mediated sorting of INPP5E into the cilium is determined by cargo-carrier affinity.,Fansa EK, Kosling SK, Zent E, Wittinghofer A, Ismail S Nat Commun. 2016 Apr 11;7:11366. doi: 10.1038/ncomms11366. PMID:27063844<ref>PMID:27063844</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5f2u" style="background-color:#fffaf0;"></div> |
| - | [[Category: Fansa | + | |
| - | [[Category: Isamil | + | ==See Also== |
| + | *[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fansa EK]] | ||
| + | [[Category: Isamil S]] | ||
| + | [[Category: Wittinghofer A]] | ||
Current revision
Structure of Fully modified farnesylated INPP5E Peptide in complex with PDE6D
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