Architecture of the native major royal jelly protein 1 oligomer

Major royal jelly protein 1 (MRJP1) is the most abundant glycoprotein in royal jelly (RJ). Here the authors isolated MRJP1 from RJ and determined the 2.65 Å resolution crystal structure of the 16-molecule oligomer, which also contained 24-methylenecholesterol and apisimin bound to MRJP1.

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Autores principales: Wenli Tian, Min Li, Huiyuan Guo, Wenjun Peng, Xiaofeng Xue, Yifan Hu, Yang Liu, Yazhou Zhao, Xiaoming Fang, Kai Wang, Xiuting Li, Yufeng Tong, Michael A. Conlon, Wei Wu, Fazheng Ren, Zhongzhou Chen
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/1dbb3c0d22e34903834dbf9853001c1e
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spelling oai:doaj.org-article:1dbb3c0d22e34903834dbf9853001c1e2021-12-02T14:39:09ZArchitecture of the native major royal jelly protein 1 oligomer10.1038/s41467-018-05619-12041-1723https://doaj.org/article/1dbb3c0d22e34903834dbf9853001c1e2018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05619-1https://doaj.org/toc/2041-1723Major royal jelly protein 1 (MRJP1) is the most abundant glycoprotein in royal jelly (RJ). Here the authors isolated MRJP1 from RJ and determined the 2.65 Å resolution crystal structure of the 16-molecule oligomer, which also contained 24-methylenecholesterol and apisimin bound to MRJP1.Wenli TianMin LiHuiyuan GuoWenjun PengXiaofeng XueYifan HuYang LiuYazhou ZhaoXiaoming FangKai WangXiuting LiYufeng TongMichael A. ConlonWei WuFazheng RenZhongzhou ChenNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Wenli Tian
Min Li
Huiyuan Guo
Wenjun Peng
Xiaofeng Xue
Yifan Hu
Yang Liu
Yazhou Zhao
Xiaoming Fang
Kai Wang
Xiuting Li
Yufeng Tong
Michael A. Conlon
Wei Wu
Fazheng Ren
Zhongzhou Chen
Architecture of the native major royal jelly protein 1 oligomer
description Major royal jelly protein 1 (MRJP1) is the most abundant glycoprotein in royal jelly (RJ). Here the authors isolated MRJP1 from RJ and determined the 2.65 Å resolution crystal structure of the 16-molecule oligomer, which also contained 24-methylenecholesterol and apisimin bound to MRJP1.
format article
author Wenli Tian
Min Li
Huiyuan Guo
Wenjun Peng
Xiaofeng Xue
Yifan Hu
Yang Liu
Yazhou Zhao
Xiaoming Fang
Kai Wang
Xiuting Li
Yufeng Tong
Michael A. Conlon
Wei Wu
Fazheng Ren
Zhongzhou Chen
author_facet Wenli Tian
Min Li
Huiyuan Guo
Wenjun Peng
Xiaofeng Xue
Yifan Hu
Yang Liu
Yazhou Zhao
Xiaoming Fang
Kai Wang
Xiuting Li
Yufeng Tong
Michael A. Conlon
Wei Wu
Fazheng Ren
Zhongzhou Chen
author_sort Wenli Tian
title Architecture of the native major royal jelly protein 1 oligomer
title_short Architecture of the native major royal jelly protein 1 oligomer
title_full Architecture of the native major royal jelly protein 1 oligomer
title_fullStr Architecture of the native major royal jelly protein 1 oligomer
title_full_unstemmed Architecture of the native major royal jelly protein 1 oligomer
title_sort architecture of the native major royal jelly protein 1 oligomer
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/1dbb3c0d22e34903834dbf9853001c1e
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