4f1m

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==Crystal Structure of the G1179S Roco4 Kinase Domain bound to AppCp from D. discoideum.==
==Crystal Structure of the G1179S Roco4 Kinase Domain bound to AppCp from D. discoideum.==
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<StructureSection load='4f1m' size='340' side='right' caption='[[4f1m]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
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<StructureSection load='4f1m' size='340' side='right'caption='[[4f1m]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F1M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4f1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F1M 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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.04&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f0f|4f0f]], [[4f0g|4f0g]], [[4f1o|4f1o]], [[4f1t|4f1t]]</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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0288251, roco4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</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=4f1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1m OCA], [https://pdbe.org/4f1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f1m RCSB], [https://www.ebi.ac.uk/pdbsum/4f1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1m ProSAT]</span></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/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=4f1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1m OCA], [http://pdbe.org/4f1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f1m RCSB], [http://www.ebi.ac.uk/pdbsum/4f1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1m ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/ROCO4_DICDI ROCO4_DICDI]
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Mutations in human leucine-rich-repeat kinase 2 (LRRK2) have been found to be the most frequent cause of late-onset Parkinson disease. Here we show that Dictyostelium discoideum Roco4 is a suitable model to study the structural and biochemical characteristics of the LRRK2 kinase and can be used for optimization of current and identification of new LRRK2 inhibitors. We have solved the structure of Roco4 kinase wild-type, Parkinson disease-related mutants G1179S and L1180T (G2019S and I2020T in LRRK2) and the structure of Roco4 kinase in complex with the LRRK2 inhibitor H1152. Taken together, our data give important insight in the LRRK2 activation mechanism and, most importantly, explain the G2019S-related increase in LRRK2 kinase activity.
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Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations.,Gilsbach BK, Ho FY, Vetter IR, van Haastert PJ, Wittinghofer A, Kortholt A Proc Natl Acad Sci U S A. 2012 Jun 11. PMID:22689969<ref>PMID:22689969</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 4f1m" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
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*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 11735]]
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[[Category: Dictyostelium discoideum]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Gilsbach, B K]]
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[[Category: Gilsbach BK]]
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[[Category: Kortholt, A]]
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[[Category: Kortholt A]]
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[[Category: Vetter, I R]]
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[[Category: Vetter IR]]
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[[Category: Wittinghofer, A]]
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[[Category: Wittinghofer A]]
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[[Category: Atp-binding]]
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[[Category: Kinase]]
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[[Category: Lrrk2]]
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[[Category: Nucleotide-binding]]
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[[Category: Protein kinase]]
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[[Category: Roco]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: Signaling protein]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of the G1179S Roco4 Kinase Domain bound to AppCp from D. discoideum.

PDB ID 4f1m

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