2h14
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(New page: 200px<br /> <applet load="2h14" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h14, resolution 1.48Å" /> '''Crystal of WDR5 (ap...)
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Revision as of 20:18, 12 November 2007
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Crystal of WDR5 (apo-form)
Contents |
Overview
The WD40-repeat protein WDR5 is a conserved subunit of Trithorax (TRX), histone methyltransferase complexes. WDR5 has been reported to selectively, bind dimethylated Lys4 (K4me2) in histone H3 to promote K4 trimethylation, by TRX. To elucidate the basis of this binding specificity, we have, determined the crystal structure of WDR5 bound to a histone H3 peptide, bearing K4me2. The structure reveals that the N terminus of histone H3, binds as a 3(10)-helix in the central depression formed by the WD40, repeats. R2 in histone H3 is bound in the acidic channel in the protein's, core, whereas K4me2 is solvent exposed and does not engage in direct, interactions with WDR5. Functional studies confirm that WDR5 recognizes, A1, R2 and T3 in histone H3 but has virtually identical affinities for the, unmodified and mono-, di- and trimethylated forms of K4, demonstrating, that it does not discriminate among different degrees of methylation of, this residue.
Disease
Known disease associated with this structure: Asphyxiating thoracic dystrophy OMIM:[611177]
About this Structure
2H14 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular recognition of histone H3 by the WD40 protein WDR5., Couture JF, Collazo E, Trievel RC, Nat Struct Mol Biol. 2006 Aug;13(8):698-703. Epub 2006 Jul 9. PMID:16829960
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