Fig. 2: Cryo-EM structure of human DGAT1 in complex with T863.
From: Mechanism of action for small-molecule inhibitors of triacylglycerol synthesis
a Ribbon representation of the human DGAT1 structure bound to T863 (green sticks). The EM density of T863 is depicted as a blue surface. The dashed line indicates a disordered segment in DGAT1 that is not resolved in the cryo-EM map. The complex structure is shown along the membrane plane and from the cytosolic side. b Zoomed-in view of intermolecular interactions between T863 with DGAT1. The blue surface represents the EM density of T863. Residues interacting with T863 are shown in orange. The catalytic residues His415 and Asn378 are labeled in red. c Two-dimensional interaction diagram for T863. Polar interactions are shown with dashed lines. Residues participating in non-polar interactions with T863 are shown as spiked arcs. d Comparison of the EM density at the fatty acyl CoA binding tunnel in apo DGAT1 (purple surface in apo-DGAT1, EMDB: 21461, PDB: 6VYI), oleoyl CoA-bound DGAT1 (orange surface in DGAT1-Oleoyl CoA, EMDB: 21481, PDB: 6VZ1)13. The EM maps in each state are contoured at 3.5σ.
