| Literature DB >> 18084306 |
Joseph Lee1, James R Thompson, Maria Victoria Botuyan, Georges Mer.
Abstract
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.Entities:
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Year: 2007 PMID: 18084306 PMCID: PMC2211384 DOI: 10.1038/nsmb1326
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369