中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
首页 机构 成果 学者
  
  1. CAS IR Grid
  2. 高能物理研究所
  3. 中国科学院高能物理研究所
  4. 多学科研究中心
Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein

文献类型：期刊论文

作者Zheng, XF; Dai, XY; Zhao, YM; Chen, Q; Lu, F; Yao, DQ; Yu, Q; Liu, XP; Zhang, CM; Gu, XC
刊名PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
出版日期2007
卷号104期号:21页码:8809-8814
关键词Rossmann fold signal transduction
通讯作者Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Dept Biochem, Beijing 100871, Peoples R China ; Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Dept Biol Mol, Beijing 100871, Peoples R China ; Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Dept Cell Biol & Genet, Beijing 100871, Peoples R China ; Chinese Acad Sci, Inst High Energy Phys, Beijing 100049, Peoples R China ; Univ Alabama, Dept Microbiol, Birmingham, AL 35294 USA
英文摘要NAD(P) has long been known as an essential energy-carrying molecule in cells. Recent data, however, indicate that NAD(P) also plays critical signaling roles in regulating cellular functions. The crystal structure of a human protein, HSCARG, with functions previously unknown, has been determined to 2.4-angstrom resolution. The structure reveals that HSCARG can form an asymmetrical dinner with one subunit occupied by one NADP molecule and the other empty. Restructuring of its NAD(P)-binding Rossmann fold upon NADP binding changes an extended loop to an a-helix to restore the integrity of the Rossmann fold. The previously unobserved restructuring suggests that HISCARG may assume a resting state when the level of NADP(H) is normal within the cell. When the NADP(H) level passes a threshold, an extensive restructuring of HSCARG would result in the activation of its regulatory functions. Immunofluorescent imaging shows that HISCARG redistributes from being associated with intermediate filaments in the resting state to being dispersed in the nucleus and the cytoplasm. The structural change of HSCARG upon NADP(H) binding could be a new regulatory mechanism that responds only to a significant change of NADP(H) levels. One of the functions regulated by HSCARG may be argininosuccinate synthetase that is involved in NO synthesis.
学科主题Science & Technology - Other Topics
类目[WOS]Multidisciplinary Sciences
研究领域[WOS]Science & Technology - Other Topics
原文出处SCI
语种英语
WOS记录号WOS:000246853700025
源URL[http://ir.ihep.ac.cn/handle/311005/240153]  
专题高能物理研究所_多学科研究中心
作者单位中国科学院高能物理研究所
推荐引用方式
GB/T 7714		 Zheng, XF,Dai, XY,Zhao, YM,et al. Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2007,104(21):8809-8814.
APA Zheng, XF.,Dai, XY.,Zhao, YM.,Chen, Q.,Lu, F.,...&姚德强.(2007).Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,104(21),8809-8814.
MLA Zheng, XF,et al."Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 104.21(2007):8809-8814.

入库方式： OAI收割

来源：高能物理研究所

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。