Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition

Mimasu et al. report a rat full-length structure of kynurenine 3-monooxygenase (KMO) in its membrane-embedded form, complexed with two inhibitors. They find that the dimeric interface of KMO is critical for its activity. This study provides insights into the drug development strategies that target K...

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Autores principales:	Shinya Mimasu, Hiroaki Yamagishi, Satoshi Kubo, Mie Kiyohara, Toshihiro Matsuda, Toshiko Yahata, Heather A. Thomson, Christopher D. Hupp, Julie Liu, Takao Okuda, Kenichi Kakefuda
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/6e58b6005eed4d88a8484826be69489a
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spelling	oai:doaj.org-article:6e58b6005eed4d88a8484826be69489a2021-12-02T14:06:19ZFull-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition10.1038/s42003-021-01666-52399-3642https://doaj.org/article/6e58b6005eed4d88a8484826be69489a2021-02-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01666-5https://doaj.org/toc/2399-3642Mimasu et al. report a rat full-length structure of kynurenine 3-monooxygenase (KMO) in its membrane-embedded form, complexed with two inhibitors. They find that the dimeric interface of KMO is critical for its activity. This study provides insights into the drug development strategies that target KMO, an important regulator of tryptophan metabolism.Shinya MimasuHiroaki YamagishiSatoshi KuboMie KiyoharaToshihiro MatsudaToshiko YahataHeather A. ThomsonChristopher D. HuppJulie LiuTakao OkudaKenichi KakefudaNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Shinya Mimasu Hiroaki Yamagishi Satoshi Kubo Mie Kiyohara Toshihiro Matsuda Toshiko Yahata Heather A. Thomson Christopher D. Hupp Julie Liu Takao Okuda Kenichi Kakefuda Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
description	Mimasu et al. report a rat full-length structure of kynurenine 3-monooxygenase (KMO) in its membrane-embedded form, complexed with two inhibitors. They find that the dimeric interface of KMO is critical for its activity. This study provides insights into the drug development strategies that target KMO, an important regulator of tryptophan metabolism.
format	article
author	Shinya Mimasu Hiroaki Yamagishi Satoshi Kubo Mie Kiyohara Toshihiro Matsuda Toshiko Yahata Heather A. Thomson Christopher D. Hupp Julie Liu Takao Okuda Kenichi Kakefuda
author_facet	Shinya Mimasu Hiroaki Yamagishi Satoshi Kubo Mie Kiyohara Toshihiro Matsuda Toshiko Yahata Heather A. Thomson Christopher D. Hupp Julie Liu Takao Okuda Kenichi Kakefuda
author_sort	Shinya Mimasu
title	Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
title_short	Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
title_full	Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
title_fullStr	Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
title_full_unstemmed	Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
title_sort	full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6e58b6005eed4d88a8484826be69489a
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Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition

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