4do0

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{{STRUCTURE_4do0| PDB=4do0 | SCENE= }}
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==Crystal Structure of human PHF8 in complex with Daminozide==
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===Crystal Structure of human PHF8 in complex with Daminozide===
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<StructureSection load='4do0' size='340' side='right' caption='[[4do0]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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{{ABSTRACT_PUBMED_022724510}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4do0]] is a 1 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=4DO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO0 FirstGlance]. <br>
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==Disease==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DZA:DAMINOZIDE'>DZA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[http://www.uniprot.org/uniprot/PHF8_HUMAN PHF8_HUMAN]] Defects in PHF8 are the cause of mental retardation syndromic X-linked Siderius type (MRXSSD) [MIM:[http://omim.org/entry/300263 300263]]. A disorder characterized by mild to borderline mental retardation with or without cleft lip/cleft palate.<ref>PMID:20548336</ref><ref>PMID:20346720</ref><ref>PMID:20421419</ref><ref>PMID:20208542</ref><ref>PMID:20622853</ref><ref>PMID:20622854</ref><ref>PMID:20101266</ref><ref>PMID:16199551</ref><ref>PMID:17661819</ref>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHF8, KIAA1111, ZNF422 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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=4do0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4do0 RCSB], [http://www.ebi.ac.uk/pdbsum/4do0 PDBsum]</span></td></tr>
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==Function==
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</table>
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[[http://www.uniprot.org/uniprot/PHF8_HUMAN PHF8_HUMAN]] Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3.<ref>PMID:20531378</ref><ref>PMID:20548336</ref><ref>PMID:19843542</ref><ref>PMID:20346720</ref><ref>PMID:20421419</ref><ref>PMID:20208542</ref><ref>PMID:20622853</ref><ref>PMID:20622854</ref><ref>PMID:20101266</ref><ref>PMID:20023638</ref>
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== Disease ==
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[[http://www.uniprot.org/uniprot/PHF8_HUMAN PHF8_HUMAN]] Defects in PHF8 are the cause of mental retardation syndromic X-linked Siderius type (MRXSSD) [MIM:[http://omim.org/entry/300263 300263]]. A disorder characterized by mild to borderline mental retardation with or without cleft lip/cleft palate.<ref>PMID:20548336</ref> <ref>PMID:20346720</ref> <ref>PMID:20421419</ref> <ref>PMID:20208542</ref> <ref>PMID:20622853</ref> <ref>PMID:20622854</ref> <ref>PMID:20101266</ref> <ref>PMID:16199551</ref> <ref>PMID:17661819</ref>
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==About this Structure==
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== Function ==
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[[4do0]] is a 1 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=4DO0 OCA].
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[[http://www.uniprot.org/uniprot/PHF8_HUMAN PHF8_HUMAN]] Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3.<ref>PMID:20531378</ref> <ref>PMID:20548336</ref> <ref>PMID:19843542</ref> <ref>PMID:20346720</ref> <ref>PMID:20421419</ref> <ref>PMID:20208542</ref> <ref>PMID:20622853</ref> <ref>PMID:20622854</ref> <ref>PMID:20101266</ref> <ref>PMID:20023638</ref>
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== References ==
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==Reference==
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<references/>
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<references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith, C H]]
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[[Category: Bountra, C.]]
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[[Category: Bountra, C]]
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[[Category: Chowdhury, R.]]
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[[Category: Chowdhury, R]]
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[[Category: Daniel, M.]]
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[[Category: Daniel, M]]
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[[Category: Delft, F von.]]
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[[Category: Delft, F von]]
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[[Category: Edwards, A.]]
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[[Category: Edwards, A]]
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[[Category: Kawamura, A.]]
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[[Category: Kawamura, A]]
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[[Category: Krojer, T.]]
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[[Category: Krojer, T]]
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[[Category: McDonough, M A.]]
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[[Category: McDonough, M A]]
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[[Category: Muller-Knapp, S.]]
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[[Category: Muller-Knapp, S]]
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[[Category: Ng, S S.]]
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[[Category: Ng, S S]]
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[[Category: Oppermann, U.]]
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[[Category: Oppermann, U]]
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[[Category: SGC, Structural Genomics Consortium.]]
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[[Category: Structural genomic]]
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[[Category: Schofield, C J.]]
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[[Category: Schofield, C J]]
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[[Category: Walport, L J.]]
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[[Category: Walport, L J]]
[[Category: Daminozide]]
[[Category: Daminozide]]
[[Category: Epigenetic]]
[[Category: Epigenetic]]

Revision as of 10:07, 21 December 2014

Crystal Structure of human PHF8 in complex with Daminozide

4do0, resolution 2.55Å

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