5e8f

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==Structure of Fully modified geranylgeranylated PDE6C Peptide in complex with PDE6D==
==Structure of Fully modified geranylgeranylated PDE6C Peptide in complex with PDE6D==
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<StructureSection load='5e8f' size='340' side='right' caption='[[5e8f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='5e8f' size='340' side='right'caption='[[5e8f]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5e8f]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E8F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E8F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5e8f]] 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=5E8F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E8F FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene></td></tr>
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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]] 2.1&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMT:O-METHYLCYSTEINE'>CMT</scene></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=CMT:O-METHYLCYSTEINE'>CMT</scene>, <scene name='pdbligand=GER:GERAN-8-YL+GERAN'>GER</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3',5'-cyclic-GMP_phosphodiesterase 3',5'-cyclic-GMP phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.35 3.1.4.35] </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=5e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8f OCA], [https://pdbe.org/5e8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e8f RCSB], [https://www.ebi.ac.uk/pdbsum/5e8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e8f ProSAT]</span></td></tr>
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<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=5e8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e8f OCA], [http://pdbe.org/5e8f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e8f RCSB], [http://www.ebi.ac.uk/pdbsum/5e8f PDBsum]</span></td></tr>
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</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/PDE6C_HUMAN PDE6C_HUMAN]] Progressive cone dystrophy;Achromatopsia. The disease is caused by mutations affecting the gene represented in this entry.
 
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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This study shows that the prenylated C-terminus of RPGR can bind to PDE6delta with high affinity, suggesting two distinct binding sites of the RPGR/PDE6delta complex. The serine residue at the -3 position relative to the prenylated cysteine seems to play a key role in defining the selectivity of PDE6delta towards ciliary prenylated cargo. [Image: see text]
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The N- and C-terminal ends of RPGR can bind to PDE6delta.,Fansa EK, O'Reilly NJ, Ismail S, Wittinghofer A EMBO Rep. 2015 Dec;16(12):1583-5. doi: 10.15252/embr.201541404. Epub 2015 Nov 9. PMID:26553937<ref>PMID:26553937</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 5e8f" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 3',5'-cyclic-GMP phosphodiesterase]]
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[[Category: Homo sapiens]]
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[[Category: Fansa, E K]]
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[[Category: Large Structures]]
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[[Category: Ismail, S A]]
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[[Category: Fansa EK]]
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[[Category: Reilly, N J.O]]
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[[Category: Ismail SA]]
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[[Category: Wittinghofer, A]]
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[[Category: O'Reilly NJ]]
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[[Category: Geranylgeranyl]]
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[[Category: Wittinghofer A]]
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[[Category: Hydrolase]]
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[[Category: Immunoglobulin-like beta sandwitch fold]]
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[[Category: Prenyl binding protein]]
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Current revision

Structure of Fully modified geranylgeranylated PDE6C Peptide in complex with PDE6D

PDB ID 5e8f

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