3qwv

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'''Unreleased structure'''
 
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The entry 3qwv is ON HOLD until Paper Publication
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==Crystal structure of histone lysine methyltransferase SmyD2 in complex with the cofactor product AdoHcy==
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<StructureSection load='3qwv' size='340' side='right'caption='[[3qwv]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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Authors: Jiang, Y., Sirinupong, N., Brunzelle, J., Yang, Z.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3qwv]] 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=3QWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QWV FirstGlance]. <br>
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Description: Crystal structure of histone lysine methyltransferase SmyD2 in complex with the cofactor product AdoHcy
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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]] 2.03&#8491;</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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3qwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qwv OCA], [https://pdbe.org/3qwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qwv RCSB], [https://www.ebi.ac.uk/pdbsum/3qwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qwv ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Brunzelle J]]
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[[Category: Jiang Y]]
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[[Category: Sirinupong N]]
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[[Category: Yang Z]]

Current revision

Crystal structure of histone lysine methyltransferase SmyD2 in complex with the cofactor product AdoHcy

PDB ID 3qwv

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