Fig. 4: The dimer interface of hSOAT1 dimer. | Nature Communications

Fig. 4: The dimer interface of hSOAT1 dimer.

From: Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor

Fig. 4

a, b Top view and side view of one hSOAT1 dimer are shown in surface representation with semi-transparency. M1, M6 and M9 helices are shown as ribbons. c Close-up view of the dimer interface boxed by solid lines in b. Interacting residues were shown in sticks. Residues mutated in f were shown in orange. d A 180° rotated view compared to c. e Close-up view of the interacting residues boxed by dashed lines in b. f FSEC traces of hSOAT1 dimer with interface mutations. g The activities of hSOAT1 dimer mutants measured using NBD-cholesterol as substrate, in the presence of cholesterol. Source data are provided as a Source Data file (Data are shown as means ± standard deviations, n = 3 biologically independent samples).

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