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- W3025883970 abstract "Abstract Sterol O -acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multi-transmembrane enzyme that belongs to the membrane-bound O -acyltransferase (MBOAT) family. It catalyzes the esterification of cholesterol to generate cholesteryl esters for cholesterol storage. SOAT1 is a target to treat several human diseases. However, its structure and mechanism remain elusive since its discovery. Here, we report the structure of human SOAT1 (hSOAT1) determined by cryo-EM. hSOAT1 is a tetramer consisted of a dimer of dimer. The structure of hSOAT1 dimer at 3.5 Å resolution reveals that a small molecule inhibitor CI-976 binds inside the catalytic chamber and blocks the accessibility of the active site residues H460, N421 and W420. Our results pave the way for future mechanistic study and rational drug design targeting hSOAT1 and other mammalian MBOAT family members." @default.
- W3025883970 created "2020-05-21" @default.
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- W3025883970 date "2020-05-18" @default.
- W3025883970 modified "2023-10-16" @default.
- W3025883970 title "Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor" @default.
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- W3025883970 doi "https://doi.org/10.1038/s41467-020-16288-4" @default.
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