7uva
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of KDM2A histone demethylase catalytic domain in complex with an H3C36 peptide modified by UNC8015== | |
- | + | <StructureSection load='7uva' size='340' side='right'caption='[[7uva]], [[Resolution|resolution]] 1.98Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[7uva]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UVA FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=OH0:N-heptanoyl-N-hydroxy-beta-alanine'>OH0</scene></td></tr> | |
- | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7uva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uva OCA], [https://pdbe.org/7uva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uva RCSB], [https://www.ebi.ac.uk/pdbsum/7uva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uva ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/KDM2A_MOUSE KDM2A_MOUSE] Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis (By similarity). | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Azzam DN]] | ||
+ | [[Category: Budziszewski GR]] | ||
+ | [[Category: Foley CA]] | ||
+ | [[Category: Frye SV]] | ||
+ | [[Category: James LI]] | ||
+ | [[Category: McGinty RK]] | ||
+ | [[Category: Skrajna A]] | ||
+ | [[Category: Spangler CJ]] |
Revision as of 12:32, 22 February 2023
Crystal structure of KDM2A histone demethylase catalytic domain in complex with an H3C36 peptide modified by UNC8015
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Categories: Homo sapiens | Large Structures | Mus musculus | Azzam DN | Budziszewski GR | Foley CA | Frye SV | James LI | McGinty RK | Skrajna A | Spangler CJ