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4f1t

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Crystal Structure of the Roco4 Kinase Domain from D. discoideum bound to the ROCK Inhibitor H1152

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 ==Crystal Structure of the Roco4 Kinase Domain from D. discoideum bound to the ROCK Inhibitor H1152==
-<StructureSection load='4f1t' size='340' side='right' caption='[[4f1t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4f1t' size='340' side='right'caption='[[4f1t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4f1t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F1T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4f1t]] 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=4F1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F1T FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H52:(S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE'>H52</scene><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]] 2.3&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f0f|4f0f]], [[4f0g|4f0g]], [[4f1m|4f1m]], [[4f1o|4f1o]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H52:(S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE'>H52</scene></td></tr>
-<tr><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 Dictyostelium discoideum])</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=4f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1t OCA], [https://pdbe.org/4f1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f1t RCSB], [https://www.ebi.ac.uk/pdbsum/4f1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f1t ProSAT]</span></td></tr>
-<tr><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>
+</table>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f1t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f1t RCSB], [http://www.ebi.ac.uk/pdbsum/4f1t PDBsum]</span></td></tr>
+== Function ==
-<table>
+[https://www.uniprot.org/uniprot/ROCO4_DICDI ROCO4_DICDI]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Dictyostelium discoideum]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Large Structures]]
-[[Category: Gilsbach, B K.]]
+[[Category: Gilsbach BK]]
-[[Category: Kortholt, A.]]
+[[Category: Kortholt A]]
-[[Category: Vetter, I R.]]
+[[Category: Vetter IR]]
-[[Category: Wittinghofer, A.]]
+[[Category: Wittinghofer A]]
-[[Category: Atp-binding]]
-[[Category: Kinase]]
-[[Category: Lrrk2]]
-[[Category: Nucleotide-binding]]
-[[Category: Protein kinase]]
-[[Category: Roco]]
-[[Category: Serine/threonine-protein kinase]]
-[[Category: Signaling protein]]
-[[Category: Signaling protein-inhibitor complex]]
-[[Category: Transferase]]

4f1t

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Crystal Structure of the Roco4 Kinase Domain from D. discoideum bound to the ROCK Inhibitor H1152

Structural highlights

Function

See Also

Contents

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