3kqi
From Proteopedia
Line 1: | Line 1: | ||
- | {{Seed}} | ||
- | [[Image:3kqi.png|left|200px]] | ||
- | |||
- | <!-- | ||
- | The line below this paragraph, containing "STRUCTURE_3kqi", creates the "Structure Box" on the page. | ||
- | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
- | or leave the SCENE parameter empty for the default display. | ||
- | --> | ||
{{STRUCTURE_3kqi| PDB=3kqi | SCENE= }} | {{STRUCTURE_3kqi| PDB=3kqi | SCENE= }} | ||
- | |||
===crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide=== | ===crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide=== | ||
+ | {{ABSTRACT_PUBMED_20129925}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/PHF2_HUMAN PHF2_HUMAN]] Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA.<ref>PMID:21532585</ref> <ref>PMID:20129925</ref> <ref>PMID:21167174</ref> | |
- | + | ||
- | + | ||
- | --> | + | |
- | + | ||
==About this Structure== | ==About this Structure== | ||
- | + | [[3kqi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KQI OCA]. | |
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020129925</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lee, M.]] | [[Category: Lee, M.]] | ||
Line 35: | Line 22: | ||
[[Category: Phd finger]] | [[Category: Phd finger]] | ||
[[Category: Zinc-finger]] | [[Category: Zinc-finger]] | ||
- | |||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 09:16:33 2010'' |
Revision as of 02:14, 4 April 2013
Contents |
crystal structure of PHF2 PHD domain complexed with H3K4Me3 peptide
Template:ABSTRACT PUBMED 20129925
Function
[PHF2_HUMAN] Lysine demethylase that demethylates both histones and non-histone proteins. Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B. Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes. The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA.[1] [2] [3]
About this Structure
3kqi is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Wen H, Li J, Song T, Lu M, Kan PY, Lee MG, Sha B, Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J Biol Chem. 2010 Mar 26;285(13):9322-6. Epub 2010 Feb 2. PMID:20129925 doi:10.1074/jbc.C109.097667
- ↑ Baba A, Ohtake F, Okuno Y, Yokota K, Okada M, Imai Y, Ni M, Meyer CA, Igarashi K, Kanno J, Brown M, Kato S. PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B. Nat Cell Biol. 2011 Jun;13(6):668-75. doi: 10.1038/ncb2228. Epub 2011 May 1. PMID:21532585 doi:10.1038/ncb2228
- ↑ Wen H, Li J, Song T, Lu M, Kan PY, Lee MG, Sha B, Shi X. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J Biol Chem. 2010 Mar 26;285(13):9322-6. Epub 2010 Feb 2. PMID:20129925 doi:10.1074/jbc.C109.097667
- ↑ Horton JR, Upadhyay AK, Hashimoto H, Zhang X, Cheng X. Structural Basis for Human PHF2 Jumonji Domain Interaction with Metal Ions. J Mol Biol. 2010 Dec 15. PMID:21167174 doi:10.1016/j.jmb.2010.12.013
Categories: Homo sapiens | Lee, M. | Li, J Z. | Lu, M. | Song, T. | Wen, H. | Histone-binding | Metal-binding | Nuclear protein | Phd finger | Zinc-finger