3b95
EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)
OverviewOverview
Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.
DiseaseDisease
Known disease associated with this structure: Chromosome 9q subtelomeric deletion syndrome OMIM:[607001]
About this StructureAbout this Structure
3B95 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules., Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X, Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10. PMID:18264113 Page seeded by OCA on Sun May 4 20:32:20 2008