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

Sterol O-acyltransferase 1 (SOAT1, also named ACAT1) is an endoplasmic reticulum resident enzyme which catalyzes the esterification of cholesterol to generate cholesteryl esters. Here, authors report cryo-EM structures of human SOAT1 which reveal the binding site of the competitive inhibitor CI-976.

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Autores principales: Chengcheng Guan, Yange Niu, Si-Cong Chen, Yunlu Kang, Jing-Xiang Wu, Koji Nishi, Catherine C. Y. Chang, Ta-Yuan Chang, Tuoping Luo, Lei Chen
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/358be672ffd24c55bc5303397e78ae42
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spelling oai:doaj.org-article:358be672ffd24c55bc5303397e78ae422021-12-02T16:51:34ZStructural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor10.1038/s41467-020-16288-42041-1723https://doaj.org/article/358be672ffd24c55bc5303397e78ae422020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16288-4https://doaj.org/toc/2041-1723Sterol O-acyltransferase 1 (SOAT1, also named ACAT1) is an endoplasmic reticulum resident enzyme which catalyzes the esterification of cholesterol to generate cholesteryl esters. Here, authors report cryo-EM structures of human SOAT1 which reveal the binding site of the competitive inhibitor CI-976.Chengcheng GuanYange NiuSi-Cong ChenYunlu KangJing-Xiang WuKoji NishiCatherine C. Y. ChangTa-Yuan ChangTuoping LuoLei ChenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Chengcheng Guan
Yange Niu
Si-Cong Chen
Yunlu Kang
Jing-Xiang Wu
Koji Nishi
Catherine C. Y. Chang
Ta-Yuan Chang
Tuoping Luo
Lei Chen
Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
description Sterol O-acyltransferase 1 (SOAT1, also named ACAT1) is an endoplasmic reticulum resident enzyme which catalyzes the esterification of cholesterol to generate cholesteryl esters. Here, authors report cryo-EM structures of human SOAT1 which reveal the binding site of the competitive inhibitor CI-976.
format article
author Chengcheng Guan
Yange Niu
Si-Cong Chen
Yunlu Kang
Jing-Xiang Wu
Koji Nishi
Catherine C. Y. Chang
Ta-Yuan Chang
Tuoping Luo
Lei Chen
author_facet Chengcheng Guan
Yange Niu
Si-Cong Chen
Yunlu Kang
Jing-Xiang Wu
Koji Nishi
Catherine C. Y. Chang
Ta-Yuan Chang
Tuoping Luo
Lei Chen
author_sort Chengcheng Guan
title Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
title_short Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
title_full Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
title_fullStr Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
title_full_unstemmed Structural insights into the inhibition mechanism of human sterol O-acyltransferase 1 by a competitive inhibitor
title_sort structural insights into the inhibition mechanism of human sterol o-acyltransferase 1 by a competitive inhibitor
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/358be672ffd24c55bc5303397e78ae42
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