3qww
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3qww is ON HOLD Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z. Description: Crystal structure of histone lysine methyltransferase SmyD...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin== | |
| - | + | <StructureSection load='3qww' size='340' side='right'caption='[[3qww]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3qww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWW 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]] 1.8Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3qww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qww OCA], [https://pdbe.org/3qww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qww RCSB], [https://www.ebi.ac.uk/pdbsum/3qww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qww ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SMYD2_MOUSE SMYD2_MOUSE] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.<ref>PMID:16805913</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Brunzelle J]] | ||
| + | [[Category: Jiang Y]] | ||
| + | [[Category: Sirinupong N]] | ||
| + | [[Category: Yang Z]] | ||
Current revision
Crystal structure of histone lysine methyltransferase SmyD2 in complex with the methyltransferase inhibitor sinefungin
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