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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.

Original publication

DOI

10.1126/science.1069473

Type

Journal article

Journal

Science (New York, N.Y.)

Publication Date

03/2002

Volume

295

Pages

2080 - 2083

Addresses

Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908-0733, USA.

Keywords

Lysine, Peptides, Drosophila Proteins, Chromosomal Proteins, Non-Histone, Histones, Crystallography, X-Ray, Sequence Alignment, Mutagenesis, Amino Acid Sequence, Amino Acid Motifs, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Binding, Methylation, Point Mutation, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data