User:Lauryn Padgett/Sandbox 1

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Structure

Overall Secondary Structure

The secondary structure is composed of 10% and 37% . The helical composition includes 3 , with two residing in the SET domain and one in the C-terminal domain. The alpha helices in the SET domain are two turns while the C-terminal helix is by far the largest with 4 turns. There are also 2 in the SET domain which are each one turn. There are 21 total beta strands which reside in the N-terminal domain and the SET domain. The beta strands are primarily anti-parallel and multiple antiparallel strands are connected by and beta turns.

The of the protein is essential for the binding and stabilization of the cofactor. The

SET Domain

Cofactor

Active Site

Mechanism

Function

Inhibitor

Sinefungin is a potent methyltransferase inhibitor. It is a structural analog of S-andeosylmethionine that is more stable due to the ability to create two additional hydrogen bonds to its amine group in the active site. It has been used experimentally to inhibit the SET 7/9 protein on peritoneal fibrosis in mice and in human peritoneal mesothelial cells.