2pxj

From Proteopedia

Revision as of 12:43, 23 January 2008

The complex structure of JMJD2A and monomethylated H3K36 peptide

Overview

The Jumonji C domain is a catalytic motif that mediates histone lysine, demethylation. The Jumonji C-containing oxygenase JMJD2A specifically, demethylates tri- and dimethylated lysine-9 and lysine-36 of histone 3, (H3K9/36me3/2). Here we present structures of the JMJD2A catalytic core, complexed with methylated H3K36 peptide substrates in the presence of, Fe(II) and N-oxalylglycine. We found that the interaction between JMJD2A, and peptides largely involves the main chains of the enzyme and the, peptide. The peptide-binding specificity is primarily determined by the, primary structure of the peptide, which explains the specificity of JMJD2A, for methylated H3K9 and H3K36 instead of other methylated residues such as, H3K27. The specificity for a particular methyl group, however, is affected, by multiple factors, such as space and the electrostatic environment in, the catalytic center of the enzyme. These results provide insights into, the mechanisms and specificity of histone demethylation.

About this Structure

2PXJ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of the recognition of a methylated histone tail by JMJD2A., Chen Z, Zang J, Kappler J, Hong X, Crawford F, Wang Q, Lan F, Jiang C, Whetstine J, Dai S, Hansen K, Shi Y, Zhang G, Proc Natl Acad Sci U S A. 2007 Jun 13;. PMID:17567753

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