We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail.
- Authors
Jacobs, Steven A; Khorasanizadeh, Sepideh
- Abstract
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.
- Publication
Science (New York, N.Y.), 2002, Vol 295, Issue 5562, p2080
- ISSN
1095-9203
- Publication type
Journal Article
- DOI
10.1126/science.1069473