1kne

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1kne, resolution 2.40Å

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Chromo domain of HP1 complexed with histone H3 tail containing trimethyllysine 9

Overview

The chromodomain of the HP1 family of proteins recognizes histone tails, with specifically methylated lysines. Here, we present structural, energetic, and mutational analyses of the complex between the Drosophila, HP1 chromodomain and the histone H3 tail with a methyllysine at residue 9, a modification associated with epigenetic silencing. The histone tail, inserts as a beta strand, completing the beta-sandwich architecture of the, chromodomain. The methylammonium group is caged by three aromatic side, chains, whereas adjacent residues form discerning contacts with one face, of the chromodomain. Comparison of dimethyl- and, trimethyllysine-containing complexes suggests a role for cation-pi and van, der Waals interactions, with trimethylation slightly improving the binding, affinity.

About this Structure

1KNE is a Protein complex structure of sequences from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail., Jacobs SA, Khorasanizadeh S, Science. 2002 Mar 15;295(5562):2080-3. Epub 2002 Feb 21. PMID:11859155

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