3rvh: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3rvh is ON HOLD  until May 09 2013
+==Crystal Structure of JMJD2A Complexed with Inhibitor==
+<StructureSection load='3rvh' size='340' side='right'caption='[[3rvh]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3rvh]] is a 2 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=3RVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.251&#8491;</td></tr>
+<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=HQ2:8-HYDROXY-3-(PIPERAZIN-1-YL)QUINOLINE-5-CARBOXYLIC+ACID'>HQ2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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'>[https://proteopedia.org/fgij/fg.htm?mol=3rvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvh OCA], [https://pdbe.org/3rvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvh RCSB], [https://www.ebi.ac.uk/pdbsum/3rvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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>
-Authors: King, O.N.F., Maloney, D.J., Tumber, A., Rai, G., Jadhav, A., Clifton, I.J., Heightman, T.D., Simeonov, A., McDonough, M.A., Schofield, C.J.
+==See Also==
+*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]]
-Description: Crystal Structure of JMJD2A Complexed with Inhibitor
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Clifton IJ]]
+[[Category: Heightman TD]]
+[[Category: Jadhav A]]
+[[Category: King ONF]]
+[[Category: Maloney DJ]]
+[[Category: McDonough MA]]
+[[Category: Rai G]]
+[[Category: Schofield CJ]]
+[[Category: Simeonov A]]
+[[Category: Tumber A]]