3b95: Difference between revisions

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{{Seed}}
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{{STRUCTURE_3b95|  PDB=3b95  |  SCENE=  }}  
{{STRUCTURE_3b95|  PDB=3b95  |  SCENE=  }}  


'''EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)'''
===EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)===




==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]]
[[Category: Transferase]]
[[Category: Transferase/structual protein complex]]
[[Category: Transferase/structual protein complex]]
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