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3b95

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{{STRUCTURE_3b95| PDB=3b95 | SCENE= }}
{{STRUCTURE_3b95| PDB=3b95 | SCENE= }}
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'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)'''
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===EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_18264113}}
==Disease==
==Disease==
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[[Category: Transferase]]
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[[Category: Transferase/structual protein complex]]
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Revision as of 21:03, 27 July 2008

Image:3b95.png

Template:STRUCTURE 3b95

Contents

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)

Template:ABSTRACT PUBMED 18264113

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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