5f2u: Difference between revisions

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'''Unreleased structure'''


The entry 5f2u is ON HOLD  until Paper Publication
==Structure of Fully modified farnesylated INPP5E Peptide in complex with PDE6D==
<StructureSection load='5f2u' size='340' side='right' caption='[[5f2u]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5f2u]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F2U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5f2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f2u OCA], [http://pdbe.org/5f2u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f2u RCSB], [http://www.ebi.ac.uk/pdbsum/5f2u PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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.


Authors: Fansa, E.K., Isamil, S., Wittinghofer, A.
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>


Description: Structure of Fully modified farnesylated INPP5E Peptide in complex with PDE6D
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5f2u" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fansa, E K]]
[[Category: Isamil, S]]
[[Category: Wittinghofer, A]]
[[Category: Wittinghofer, A]]
[[Category: Fansa, E.K]]
[[Category: Immunoglobulin-like]]
[[Category: Isamil, S]]
[[Category: Lipid binding protein]]
[[Category: Signaling protein]]
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