北京大学医学部机构知识库
Advanced  
IR@PKUHSC  > 基础医学院  > 免疫学系  > 期刊论文
学科主题: 基础医学
题名:
The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character
作者: 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
发表日期: 2005-11-15
DOI: 10.1042/BJ20050688
卷: 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
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/62895
Appears in Collections:基础医学院_免疫学系_期刊论文

Files in This Item:
File Name/ File Size Content Type Version Access License
47.full.pdf(688KB)期刊论文出版稿限制开放 联系获取全文

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

Recommended Citation:
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.
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Liu, DS]'s Articles
[Yao, HW]'s Articles
[Chen, YY]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Liu, DS]‘s Articles
[Yao, HW]‘s Articles
[Chen, YY]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
Add to CiteULike Add to Connotea Add to Del.icio.us Add to Digg Add to Reddit

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Copyright © 2007-2017  北京大学医学部 - Feedback
Powered by CSpace