Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Research Abstract Details 

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Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Abstract Text:

Joseph Lee,James R Thompson,Maria Victoria Botuyan,Georges Mer,

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.

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Publishing Authors By Initials

J Lee,JR Thompson,MV Botuyan,G Mer,

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Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Nature structural & molecular biology

VOLUME: 15

Page Numbers: 109-11

Journal Abbreviation: Nat. Struct. Mol. Biol.

ISSN: 1545-9985

DAY: 16

MONTH: 12

YEAR: 2007

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Information

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LANGUAGE: eng

NlmUniqueID: 101186374

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Grant and Affiliation Information for Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.

AFFILIATION: Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA.

Country: United States

AGENCY: United States NCI

GRANT: CA109449

ACRONYM: CA

MEDLINETA: Nat Struct Mol Biol

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ACCESSION NUMBER: 2QQS

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