中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP

文献类型:期刊论文

作者Hou, Meng-Meng5,6; Polykretis, Panagis4; Luchinat, Enrico3,4; Wang, Xiao5,6; Chen, Shen-Na5,6; Zuo, Hui-Hui5,6; Yang, Yin5,6; Chen, Jia-Liang5,6; Ye, Yansheng1; Li, Conggang1
刊名SCIENTIFIC REPORTS
出版日期2017-11-30
卷号7
ISSN号2045-2322
DOI10.1038/s41598-017-16723-5
文献子类Article
英文摘要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.
WOS关键词PARAMAGNETIC NMR-SPECTROSCOPY ; PROTEIN-PRODUCTION ; MAMMALIAN-CELLS ; INHIBITION ; BINDING ; APOPTOSIS ; OOCYTES
WOS研究方向Science & Technology - Other Topics
语种英语
WOS记录号WOS:000416891400032
出版者NATURE PUBLISHING GROUP
资助机构National Key R&D Program of China(2016YFA0501202) ; National Key R&D Program of China(2016YFA0501202) ; National Natural Science Foundation of China(21673122 ; National Natural Science Foundation of China(21673122 ; 21473095) ; 21473095) ; National Key R&D Program of China(2016YFA0501202) ; National Key R&D Program of China(2016YFA0501202) ; National Natural Science Foundation of China(21673122 ; National Natural Science Foundation of China(21673122 ; 21473095) ; 21473095) ; National Key R&D Program of China(2016YFA0501202) ; National Key R&D Program of China(2016YFA0501202) ; National Natural Science Foundation of China(21673122 ; National Natural Science Foundation of China(21673122 ; 21473095) ; 21473095) ; National Key R&D Program of China(2016YFA0501202) ; National Key R&D Program of China(2016YFA0501202) ; National Natural Science Foundation of China(21673122 ; National Natural Science Foundation of China(21673122 ; 21473095) ; 21473095)
源URL[http://ir.wipm.ac.cn/handle/112942/12728]  
专题中国科学院武汉物理与数学研究所
通讯作者Banci, Lucia; Su, Xun-Cheng
作者单位1.Chinese Acad Sci, Key Lab Magnet Resonance Biol Syst, State Key Lab Magnet Resonance & Atom & Mol Phys, Natl Ctr Magnet Resonance Wuhan,Wuhan Inst Phys &, Wuhan 430071, Hubei, Peoples R China
2.Univ Florence, Dept Chem, I-50019 Florence, Italy
3.Univ Florence, Dept Biomed Clin & Expt Sci, I-50134 Florence, Italy
4.Univ Florence, Magnet Resonance Ctr CERM, I-50019 Florence, Italy
5.Nankai Univ, Res Inst Elementoorgan Chem, Coll Chem, Collaborat Innovat Ctr Chem Sci & Engn Tianjin, Tianjin 300071, Peoples R China
6.Nankai Univ, State Key Lab, Tianjin 300071, Peoples R China
推荐引用方式
GB/T 7714
Hou, Meng-Meng,Polykretis, Panagis,Luchinat, Enrico,et al. Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP[J]. SCIENTIFIC REPORTS,2017,7.
APA Hou, Meng-Meng.,Polykretis, Panagis.,Luchinat, Enrico.,Wang, Xiao.,Chen, Shen-Na.,...&Su, Xun-Cheng.(2017).Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP.SCIENTIFIC REPORTS,7.
MLA Hou, Meng-Meng,et al."Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP".SCIENTIFIC REPORTS 7(2017).

入库方式: OAI收割

来源:武汉物理与数学研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。