Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition

Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition

Emopamil-Binding Protein (EBP), is an endoplasmic reticulum membrane protein involved in cholesterol biosynthesis, autophagy and oligodendrocyte formation. Here, authors report two crystal structures of human EBP and identify a pharmacological binding site that accommodates multiple different ligand...

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Autores principales: Tao Long, Abdirahman Hassan, Bonne M Thompson, Jeffrey G McDonald, Jiawei Wang, Xiaochun Li
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/94264a1396794620b380724e03025384
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spelling oai:doaj.org-article:94264a1396794620b380724e030253842021-12-02T14:40:00ZStructural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition10.1038/s41467-019-10279-w2041-1723https://doaj.org/article/94264a1396794620b380724e030253842019-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10279-whttps://doaj.org/toc/2041-1723Emopamil-Binding Protein (EBP), is an endoplasmic reticulum membrane protein involved in cholesterol biosynthesis, autophagy and oligodendrocyte formation. Here, authors report two crystal structures of human EBP and identify a pharmacological binding site that accommodates multiple different ligands.Tao LongAbdirahman HassanBonne M ThompsonJeffrey G McDonaldJiawei WangXiaochun LiNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-8 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Tao Long
Abdirahman Hassan
Bonne M Thompson
Jeffrey G McDonald
Jiawei Wang
Xiaochun Li
Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
description Emopamil-Binding Protein (EBP), is an endoplasmic reticulum membrane protein involved in cholesterol biosynthesis, autophagy and oligodendrocyte formation. Here, authors report two crystal structures of human EBP and identify a pharmacological binding site that accommodates multiple different ligands.
format article
author Tao Long
Abdirahman Hassan
Bonne M Thompson
Jeffrey G McDonald
Jiawei Wang
Xiaochun Li
author_facet Tao Long
Abdirahman Hassan
Bonne M Thompson
Jeffrey G McDonald
Jiawei Wang
Xiaochun Li
author_sort Tao Long
title Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
title_short Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
title_full Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
title_fullStr Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
title_full_unstemmed Structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
title_sort structural basis for human sterol isomerase in cholesterol biosynthesis and multidrug recognition
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/94264a1396794620b380724e03025384
work_keys_str_mv AT taolong structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
AT abdirahmanhassan structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
AT bonnemthompson structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
AT jeffreygmcdonald structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
AT jiaweiwang structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
AT xiaochunli structuralbasisforhumansterolisomeraseincholesterolbiosynthesisandmultidrugrecognition
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