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学科主题基础医学
The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character
Liu, DS; Yao, HW; Chen, YY; Feng, YG; Chen, YY; Wang, JF
关键词apoptosis electrostatic potential surface alpha-helix NMR programmed cell death 5 (PDCD5) solution structure
刊名BIOCHEMICAL JOURNAL
2005-11-15
DOI10.1042/BJ20050688
392期:0页:47-54
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]SECONDARY STRUCTURE ; CHEMICAL-SHIFT ; NMR ; PHOSPHATIDYLSERINE ; APOPTOSIS ; PEPTIDES ; TFAR19 ; CELLS ; TF-1
英文摘要

PDCD5-(1-26) is a N-terminal 26-residue fragment of human PDCD5 (programmed cell death 5) protein. PDCD5 is an important novel protein that regulates both apoptotic and nonapoptotic programmed cell death. The conformation of PDCD5 protein is a stable helical core consisting of a triple-helix bundle and two dissociated terminal regions. The N-terminal region is ordered and contains abundant secondary structure. Overexpression and purification of the N-terminal 26-residure fragment, PDCD5-(l-26), was performed in this study to better understand its tertiary structure. The spectroscopic studies using CD and hetero- and homo-nuclear NMR methods determine a stable alpha-helix formed by Asp(3)-Ala(19) of PDCD5-(1-26). The N-terminal residues Asp(3)-Ala(19) of PDCD5 were then affirmed to have the capacity to form a stable alpha-helix independently of the core of the protein. Analysis of the helical peptide of PDCD5-(1-26) indicates that the surface of this well-formed alpha-helix has a unique electrostatic potential character. This may provide an environment for the N-terminal alpha-helix of PDCD5 to serve as an independent functional entity of the protein. The apoptosis activity assay shows that the deletion of the N-terminal alpha-helix of PDCD5 significantly attenuates the apoptosis-promoting effects on HL-60 cells induced by serum withdrawal.

语种英语
WOS记录号WOS:000233542800006
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被引频次:12[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/62895
专题北京大学基础医学院_免疫学系
作者单位1.Chinese Acad Sci, Inst Biophys, Ctr Mol Biol, Natl Lab Biomacromol, Beijing 100101, Peoples R China
2.Peking Univ, Hlth Sci Ctr, Sch Basic Med Sci, Lab Med Immunol, Beijing 100083, Peoples R China
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Liu, DS,Yao, HW,Chen, YY,et al. The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character[J]. BIOCHEMICAL JOURNAL,2005,392(0):47-54.
APA Liu, DS,Yao, HW,Chen, YY,Feng, YG,Chen, YY,&Wang, JF.(2005).The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character.BIOCHEMICAL JOURNAL,392(0),47-54.
MLA Liu, DS,et al."The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character".BIOCHEMICAL JOURNAL 392.0(2005):47-54.
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