Title : Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.

Pub. Date : 2013 Apr

PMID : 23519668






3 Functional Relationships(s)
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1 Here, crystal structures of SET7/9 are reported in complexes with two AdoMet analogues, designated DAAM-3 and AAM-1, in which an n-hexylaminoethyl group or an n-hexyl group is attached to the N atom that replaces the S atom of AdoMet, respectively. Nitrogen SET domain containing 7, histone lysine methyltransferase Homo sapiens
2 The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. Nitrogen SET domain containing 7, histone lysine methyltransferase Homo sapiens
3 The N atom in the azaalkyl chain of DAAM-3 is located at almost the same position as the N-methyl C atom of the methylated lysine side chain in the substrate-peptide complex structures and stabilizes complex formation by hydrogen bonding to the substrate-binding site residues of SET7/9. Nitrogen SET domain containing 7, histone lysine methyltransferase Homo sapiens