This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4ura
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Crystal structure of human JMJD2A in complex with compound 14a== |
| - | + | <StructureSection load='4ura' size='340' side='right' caption='[[4ura]], [[Resolution|resolution]] 2.23Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ura]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4URA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4URA FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LEL:2-(2H-1,2,3-TRIAZOL-4-YL)PYRIDINE-4-CARBOXYLIC+ACID'>LEL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ura FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ura OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ura RCSB], [http://www.ebi.ac.uk/pdbsum/4ura PDBsum]</span></td></tr> | |
| - | + | </table> | |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/KDM4A_HUMAN KDM4A_HUMAN]] Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.<ref>PMID:16024779</ref> <ref>PMID:16603238</ref> <ref>PMID:21694756</ref> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arrowsmith, C H]] | ||
| + | [[Category: Bountra, C]] | ||
| + | [[Category: Brennan, P E]] | ||
[[Category: Burgess-Brown, N]] | [[Category: Burgess-Brown, N]] | ||
| + | [[Category: Crawley, L]] | ||
| + | [[Category: Edwards, A]] | ||
| + | [[Category: England, K S]] | ||
[[Category: Krojer, T]] | [[Category: Krojer, T]] | ||
| - | [[Category: Bountra, C]] | ||
| - | [[Category: Vollmar, M]] | ||
| - | [[Category: England, K.S]] | ||
| - | [[Category: Arrowsmith, C.H]] | ||
[[Category: Oppermann, U]] | [[Category: Oppermann, U]] | ||
| + | [[Category: Riesebos, E]] | ||
[[Category: Szykowska, A]] | [[Category: Szykowska, A]] | ||
| + | [[Category: Vollmar, M]] | ||
[[Category: Williams, E]] | [[Category: Williams, E]] | ||
| - | [[Category: | + | [[Category: VonDelft, F]] |
| - | [[Category: | + | [[Category: Histone demethylase]] |
| - | [[Category: | + | [[Category: Jumonjic]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
Revision as of 15:22, 17 June 2015
Crystal structure of human JMJD2A in complex with compound 14a
| |||||||||||
