5teg
From Proteopedia
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| ==Crystal structure of hSETD8 in complex with histone H4K20 norleucine mutant peptide and S-Adenosylmethionine== | ==Crystal structure of hSETD8 in complex with histone H4K20 norleucine mutant peptide and S-Adenosylmethionine== | ||
| - | <StructureSection load='5teg' size='340' side='right' caption='[[5teg]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='5teg' size='340' side='right'caption='[[5teg]], [[Resolution|resolution]] 1.30Å' scene=''> | 
| == Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5teg]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5teg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TEG FirstGlance]. <br> | 
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | 
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=5teg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5teg OCA], [https://pdbe.org/5teg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5teg RCSB], [https://www.ebi.ac.uk/pdbsum/5teg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5teg ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
| </table> | </table> | ||
| == Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/KMT5A_HUMAN KMT5A_HUMAN] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:23478445</ref>  | 
| <div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| == Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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| ==See Also== | ==See Also== | ||
| - | *[[Histone methyltransferase|Histone methyltransferase]] | + | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | 
| == References == | == References == | ||
| <references/> | <references/> | ||
| __TOC__ | __TOC__ | ||
| </StructureSection> | </StructureSection> | ||
| - | [[Category:  | + | [[Category: Homo sapiens]] | 
| - | [[Category:  | + | [[Category: Large Structures]] | 
| - | [[Category:  | + | [[Category: Judge RA]] | 
| - | [[Category:  | + | [[Category: Petros AM]] | 
| - | + | ||
| - | + | ||
Current revision
Crystal structure of hSETD8 in complex with histone H4K20 norleucine mutant peptide and S-Adenosylmethionine
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