Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 1, Pages 109-111Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1326
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Funding
- NATIONAL CANCER INSTITUTE [R01CA132878, R01CA109449] Funding Source: NIH RePORTER
- NCI NIH HHS [CA109449, R01 CA132878, R01 CA109449-04, R01 CA109449, R01 CA132878-01] Funding Source: Medline
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The lysine demethylase JMJD2A has the unique property of binding trimethylated peptides from two different histone sequences ( H3K4me3 and H4K20me3) through its tudor domains. Here we show using X-ray crystallography and calorimetry that H3K4me3 and H4K20me3, which are recognized with similar affinities by JMJD2A, adopt radically different binding modes, to the extent that we were able to design single point mutations in JMJD2A that inhibited the recognition of H3K4me3 but not H4K20me3 and vice versa.
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