3b95
From Proteopedia
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| , resolution 2.99Å | |||||||
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| Sites: | , , , , , , , and | ||||||
| Ligands: | , | ||||||
| Gene: | EHMT1 (Homo sapiens) | ||||||
| Related: | 3B7B
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)
Contents |
Overview
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.
Disease
Known disease associated with this structure: Chromosome 9q subtelomeric deletion syndrome OMIM:[607001]
About this Structure
3B95 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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