2h68
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(New page: 200px<br /> <applet load="2h68" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h68, resolution 1.79Å" /> '''Histone H3 recognit...)
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Revision as of 20:20, 12 November 2007
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Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
Contents |
Overview
WDR5 is a core component of SET1-family complexes that achieve, transcriptional activation via methylation of histone H3 on Nzeta of Lys4, (H3K4). The role of WDR5 in the MLL1 complex has recently been described, as specific recognition of dimethyl-K4 in the context of a histone H3, amino terminus; WDR5 is essential for vertebrate development, Hox gene, activation and global H3K4 trimethylation. We report the high-resolution, X-ray structures of WDR5 in the unliganded form and complexed with histone, H3 peptides having unmodified and mono-, di- and trimethylated K4, which, together provide the first comprehensive analysis of methylated histone, recognition by the ubiquitous WD40-repeat fold. Contrary to predictions, the structures reveal that WDR5 does not read out the methylation state of, K4 directly, but instead serves to present the K4 side chain for further, methylation by SET1-family complexes.
Disease
Known disease associated with this structure: Asphyxiating thoracic dystrophy OMIM:[611177]
About this Structure
2H68 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex., Ruthenburg AJ, Wang W, Graybosch DM, Li H, Allis CD, Patel DJ, Verdine GL, Nat Struct Mol Biol. 2006 Aug;13(8):704-12. Epub 2006 Jul 9. PMID:16829959
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