6mon

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Current revision (06:35, 11 October 2023) (edit) (undo)
 
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==Crystal structure of human SMYD2 in complex with Nle-peptide inhibitor==
==Crystal structure of human SMYD2 in complex with Nle-peptide inhibitor==
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<StructureSection load='6mon' size='340' side='right' caption='[[6mon]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
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<StructureSection load='6mon' size='340' side='right'caption='[[6mon]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mon]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MON OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MON FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6mon]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MON 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.711&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mon OCA], [http://pdbe.org/6mon PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mon RCSB], [http://www.ebi.ac.uk/pdbsum/6mon PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mon ProSAT]</span></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=6mon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mon OCA], [https://pdbe.org/6mon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mon RCSB], [https://www.ebi.ac.uk/pdbsum/6mon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mon ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN]] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>
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[https://www.uniprot.org/uniprot/SMYD2_HUMAN SMYD2_HUMAN] Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins. Specifically methylates histone H3 'Lys-4' (H3K4me) and dimethylates histone H3 'Lys-36' (H3K36me2). Has also methyltransferase activity toward non-histone proteins such as p53/TP53 and RB1. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates 'Lys-860' of RB1/RB.<ref>PMID:17108971</ref> <ref>PMID:17805299</ref> <ref>PMID:18065756</ref> <ref>PMID:20870719</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6mon" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6mon" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brunzelle, J]]
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[[Category: Homo sapiens]]
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[[Category: Cornett, E]]
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[[Category: Large Structures]]
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[[Category: Rothbart, S]]
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[[Category: Synthetic construct]]
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[[Category: Spellmon, N]]
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[[Category: Brunzelle J]]
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[[Category: Yang, Z]]
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[[Category: Cornett E]]
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[[Category: Complex]]
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[[Category: Rothbart S]]
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[[Category: Methyltransferase]]
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[[Category: Spellmon N]]
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[[Category: Norleucine]]
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[[Category: Yang Z]]
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[[Category: Transferase]]
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Current revision

Crystal structure of human SMYD2 in complex with Nle-peptide inhibitor

PDB ID 6mon

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