Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP

Abstract The X-chromosome linked inhibitor of apoptosis (XIAP) is a multidomain metalloprotein involved in caspase inhibition and in copper homeostasis. It contains three zinc-binding baculoviral IAP repeats (BIR) domains, which are responsible for caspase interaction. Recently, it has been suggeste...

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Autores principales:	Meng-Meng Hou, Panagis Polykretis, Enrico Luchinat, Xiao Wang, Shen-Na Chen, Hui-Hui Zuo, Yin Yang, Jia-Liang Chen, Yansheng Ye, Conggang Li, Lucia Banci, Xun-Cheng Su
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/19a844c194a644ec9b6abc7de73a76ed
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spelling	oai:doaj.org-article:19a844c194a644ec9b6abc7de73a76ed2021-12-02T15:06:27ZSolution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP10.1038/s41598-017-16723-52045-2322https://doaj.org/article/19a844c194a644ec9b6abc7de73a76ed2017-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-16723-5https://doaj.org/toc/2045-2322Abstract The X-chromosome linked inhibitor of apoptosis (XIAP) is a multidomain metalloprotein involved in caspase inhibition and in copper homeostasis. It contains three zinc-binding baculoviral IAP repeats (BIR) domains, which are responsible for caspase interaction. Recently, it has been suggested that the BIR domains can bind copper, however high resolution data on such interaction is missing. Here we characterize by NMR the structural properties of BIR1 in solution, and the effects of its interaction with copper both in vitro and in physiological environments. BIR1 is dimeric in solution, consistent with the X-ray structure. Cysteine 12, located in the unfolded N-terminal region, has a remarkably low redox potential, and is prone to oxidation even in reducing physiological environments. Interaction of BIR1 with copper(II) results in the oxidation of cysteine 12, with the formation of either an intermolecular disulfide bond between two BIR1 molecules or a mixed disulfide bond with glutathione, whereas the zinc binding site is not affected by the interaction.Meng-Meng HouPanagis PolykretisEnrico LuchinatXiao WangShen-Na ChenHui-Hui ZuoYin YangJia-Liang ChenYansheng YeConggang LiLucia BanciXun-Cheng SuNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Meng-Meng Hou Panagis Polykretis Enrico Luchinat Xiao Wang Shen-Na Chen Hui-Hui Zuo Yin Yang Jia-Liang Chen Yansheng Ye Conggang Li Lucia Banci Xun-Cheng Su Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
description	Abstract The X-chromosome linked inhibitor of apoptosis (XIAP) is a multidomain metalloprotein involved in caspase inhibition and in copper homeostasis. It contains three zinc-binding baculoviral IAP repeats (BIR) domains, which are responsible for caspase interaction. Recently, it has been suggested that the BIR domains can bind copper, however high resolution data on such interaction is missing. Here we characterize by NMR the structural properties of BIR1 in solution, and the effects of its interaction with copper both in vitro and in physiological environments. BIR1 is dimeric in solution, consistent with the X-ray structure. Cysteine 12, located in the unfolded N-terminal region, has a remarkably low redox potential, and is prone to oxidation even in reducing physiological environments. Interaction of BIR1 with copper(II) results in the oxidation of cysteine 12, with the formation of either an intermolecular disulfide bond between two BIR1 molecules or a mixed disulfide bond with glutathione, whereas the zinc binding site is not affected by the interaction.
format	article
author	Meng-Meng Hou Panagis Polykretis Enrico Luchinat Xiao Wang Shen-Na Chen Hui-Hui Zuo Yin Yang Jia-Liang Chen Yansheng Ye Conggang Li Lucia Banci Xun-Cheng Su
author_facet	Meng-Meng Hou Panagis Polykretis Enrico Luchinat Xiao Wang Shen-Na Chen Hui-Hui Zuo Yin Yang Jia-Liang Chen Yansheng Ye Conggang Li Lucia Banci Xun-Cheng Su
author_sort	Meng-Meng Hou
title	Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
title_short	Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
title_full	Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
title_fullStr	Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
title_full_unstemmed	Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP
title_sort	solution structure and interaction with copper in vitro and in living cells of the first bir domain of xiap
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/19a844c194a644ec9b6abc7de73a76ed
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Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP

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