4yzn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Humanized Roco4 bound to Compound 19== | |
| + | <StructureSection load='4yzn' size='340' side='right'caption='[[4yzn]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4yzn]] 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=4YZN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YZN 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]] 1.55Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4K5:(4-{[4-(CYCLOPROPYLAMINO)-5-(TRIFLUOROMETHYL)PYRIMIDIN-2-YL]AMINO}-2-FLUORO-5-METHOXYPHENYL)(MORPHOLIN-4-YL)METHANONE'>4K5</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=4yzn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yzn OCA], [https://pdbe.org/4yzn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yzn RCSB], [https://www.ebi.ac.uk/pdbsum/4yzn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yzn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ROCO4_DICDI ROCO4_DICDI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinase inhibition is considered to be an important therapeutic target for LRRK2 mediated Parkinson's disease (PD). Many LRRK2 kinase inhibitors have been reported but have yet to be optimized in order to qualify as drug candidates for the treatment of the disease. In order to start a structure-function analysis of such inhibitors, we mutated the active site of Dictyostelium Roco4 kinase to resemble LRRK2. Here, we show saturation transfer difference (STD) NMR and the first cocrystal structures of two potent in vitro inhibitors, LRRK2-IN-1 and compound 19, with mutated Roco4. Our data demonstrate that this system can serve as an excellent tool for the structural characterization and optimization of LRRK2 inhibitors using X-ray crystallography and NMR spectroscopy. | ||
| - | + | Structural Characterization of LRRK2 Inhibitors.,Gilsbach BK, Messias AC, Ito G, Sattler M, Alessi DR, Wittinghofer A, Kortholt A J Med Chem. 2015 May 1. PMID:25897865<ref>PMID:25897865</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4yzn" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gilsbach | + | |
| - | [[Category: Kortholt | + | ==See Also== |
| - | [[Category: | + | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dictyostelium discoideum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Alessi DR]] | ||
| + | [[Category: Gilsbach BK]] | ||
| + | [[Category: Ito G]] | ||
| + | [[Category: Kortholt A]] | ||
| + | [[Category: Messias AC]] | ||
| + | [[Category: Sattler M]] | ||
| + | [[Category: Wittinghofer A]] | ||
Current revision
Humanized Roco4 bound to Compound 19
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