5d6y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
==Crystal structure of double tudor domain of human lysine demethylase KDM4A complexed with histone H3K23me3==
-
 
+
<StructureSection load='5d6y' size='340' side='right' caption='[[5d6y]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
-
The entry 5d6y is ON HOLD
+
== Structural highlights ==
-
 
+
<table><tr><td colspan='2'>[[5d6y]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D6Y FirstGlance]. <br>
-
Authors: Wang, F., Su, Z., Miller, M.D., Denu, J.M., Phillips Jr., G.N., Enzyme Discovery for Natural Product Biosynthesis (NatPro)
+
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
-
 
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d6x|5d6x]], [[5d6w|5d6w]]</td></tr>
-
Description: Crystal structure of double tudor domain of human lysine demethylase KDM4A complexed with histone H3K23me3
+
<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=5d6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6y OCA], [http://pdbe.org/5d6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d6y RCSB], [http://www.ebi.ac.uk/pdbsum/5d6y PDBsum]</span></td></tr>
-
[[Category: Unreleased Structures]]
+
</table>
-
[[Category: G.N]]
+
== Function ==
 +
[[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: Denu, J M]]
 +
[[Category: Miller, M D]]
 +
[[Category: NatPro, Enzyme Discovery for Natural Product Biosynthesis]]
 +
[[Category: Phillips, G N]]
[[Category: Su, Z]]
[[Category: Su, Z]]
-
[[Category: Denu, J.M]]
 
-
[[Category: Enzyme Discovery For Natural Product Biosynthesis (Natpro)]]
 
[[Category: Wang, F]]
[[Category: Wang, F]]
-
[[Category: Phillips Jr]]
+
[[Category: Double tudor domain]]
-
[[Category: Miller, M.D]]
+
[[Category: Enzyme discovery for natural product biosynthesis]]
 +
[[Category: Natpro]]
 +
[[Category: Oxidoreductase]]
 +
[[Category: PSI, Protein structure initiative]]
 +
[[Category: Reader domain]]
 +
[[Category: Structural genomic]]

Revision as of 17:25, 10 February 2016

Crystal structure of double tudor domain of human lysine demethylase KDM4A complexed with histone H3K23me3

5d6y, resolution 2.29Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5d6y"
Personal tools