5fy5: Difference between revisions
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==Crystal structure of the catalytic domain of human JARID1B in complex with fumarate== | ==Crystal structure of the catalytic domain of human JARID1B in complex with fumarate== | ||
<StructureSection load='5fy5' size='340' side='right' caption='[[5fy5]], [[Resolution|resolution]] 2.47Å' scene=''> | <StructureSection load='5fy5' size='340' side='right'caption='[[5fy5]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fy5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FY5 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5fy5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FY5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FY5 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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy7|5fy7]], [[5fy8|5fy8]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyh|5fyh]], [[5fyi|5fyi]], [[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]], [[5fz6|5fz6]], [[5fz7|5fz7]], [[5fz8|5fz8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fxv|5fxv]], [[5fxw|5fxw]], [[5fxx|5fxx]], [[5fxz|5fxz]], [[5fy0|5fy0]], [[5fy1|5fy1]], [[5fy4|5fy4]], [[5fy7|5fy7]], [[5fy8|5fy8]], [[5fy9|5fy9]], [[5fyb|5fyb]], [[5fyc|5fyc]], [[5fyh|5fyh]], [[5fyi|5fyi]], [[5fym|5fym]], [[5fys|5fys]], [[5fyt|5fyt]], [[5fyu|5fyu]], [[5fyv|5fyv]], [[5fyy|5fyy]], [[5fyz|5fyz]], [[5fz0|5fz0]], [[5fz1|5fz1]], [[5fz3|5fz3]], [[5fz4|5fz4]], [[5fz6|5fz6]], [[5fz7|5fz7]], [[5fz8|5fz8]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fy5 OCA], [http://pdbe.org/5fy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fy5 RCSB], [http://www.ebi.ac.uk/pdbsum/5fy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fy5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KDM5B_HUMAN KDM5B_HUMAN]] Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.<ref>PMID:12657635</ref> <ref>PMID:16645588</ref> <ref>PMID:17320161</ref> <ref>PMID:17363312</ref> | [[http://www.uniprot.org/uniprot/KDM5B_HUMAN KDM5B_HUMAN]] Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.<ref>PMID:12657635</ref> <ref>PMID:16645588</ref> <ref>PMID:17320161</ref> <ref>PMID:17363312</ref> | ||
==See Also== | |||
*[[Jumonji domain-containing protein 3D structures|Jumonji domain-containing protein 3D structures]] | |||
*[[Lysine-specific histone demethylase 3D structures|Lysine-specific histone demethylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
