2qqs

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(New page: 200px<br /><applet load="2qqs" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qqs, resolution 2.82&Aring;" /> '''JMJD2A tandem tudor ...)
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Revision as of 08:59, 31 January 2008

Image:2qqs.jpg

2qqs, resolution 2.82Å

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JMJD2A tandem tudor domains in complex with a trimethylated histone H4-K20 peptide

Overview

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.

About this Structure

2QQS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor., Lee J, Thompson JR, Botuyan MV, Mer G, Nat Struct Mol Biol. 2008 Jan;15(1):109-11. Epub 2007 Dec 16. PMID:18084306

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