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- W4214688977 abstract "Biological responses to histone methylation critically depend on the faithful readout and transduction of the methyl-lysine signal by effector proteins, yet our understanding of methyl-lysine recognition has so far been limited to the study of histone binding by chromodomain and WD40-repeat proteins. The double tudor domain of JMJD2A, a Jmjc domain-containing histone demethylase, binds methylated histone H3-K4 and H4-K20. We found that the double tudor domain has an interdigitated structure, and the unusual fold is required for its ability to bind methylated histone tails. The cocrystal structure of the JMJD2A double tudor domain with a trimethylated H3-K4 peptide reveals that the trimethyl-K4 is bound in a cage of three aromatic residues, two of which are from the tudor-2 motif, whereas the binding specificity is determined by side-chain interactions involving amino acids from the tudor-1 motif. Our study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains. PMID: 16601153 Funding information This work was supported by: NIGMS NIH HHS, United States Grant ID: GM68804 NIGMS NIH HHS, United States Grant ID: GM 63718 NIDDK NIH HHS, United States Grant ID: DK62248" @default.
- W4214688977 created "2022-03-02" @default.
- W4214688977 creator A5046686387 @default.
- W4214688977 date "2006-05-12" @default.
- W4214688977 modified "2023-10-05" @default.
- W4214688977 title "Faculty Opinions recommendation of Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A." @default.
- W4214688977 doi "https://doi.org/10.3410/f.1032283.372960" @default.
- W4214688977 hasPublicationYear "2006" @default.
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