Human euchromatic histone methyltransferase 1, also known as G9a-like protein (or “GLP”) is a is an important Histone lysine Methyltransferase (HKMT) responsible for the methylation of Lys-9 of Histone 3.
This tour shows a closed state of the catalytic domain of GLP whereby a cofactor, SAH, (dark purple), and H3K9me (pink) are bound.
In this tour of GLP’s catalytic domain will discover how the electrostatic surface of the protein is guides interactions with the substrate, learn about the special conserved aromatic residues who’s interactions in the binding pocket appropriately orient the histone tail, observe the rigid docking platform facilitated by the I-SET backbone, and investigate the role of cofactors, SAH and Zinc, in the folding of the flexible SET-domain about the substrate.
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