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学科主题: 基础医学
题名:
Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function
作者: Shi, Di-Jing1; Ye, Sheng2; Cao, Xu1; Zhang, Rongguang2; Wang, KeWei1,3,4
关键词: TRPV3 ; ARD ; keratinocyte ; 2-APB ; skin
刊名: PROTEIN & CELL
发表日期: 2013-12-01
DOI: 10.1007/s13238-013-3091-0
卷: 4, 期:12, 页:942-950
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Cell Biology
研究领域[WOS]: Cell Biology
关键词[WOS]: ION CHANNELS ; 2-AMINOETHOXYDIPHENYL BORATE ; HEAT ; MUTATIONS ; RECEPTOR ; SKIN ; THERMOSENSATION ; SENSITIVITY ; ACTIVATION ; MICE
英文摘要:

In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular Ntermini. Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. Despite the sequence similarity among the ARDs of TRPV channels, the structure of TRPV3-ARD, however, remains unknown. Here, we report the crystal structure of TRPV3-ARD solved at 1.95 resolution, which reveals six-ankyrin repeats. While overall structure of TRPV3-ARD is similar to ARDs from other members of TRPV subfamily; it, however, features a noticeable finger 3 loop that bends over and is stabilized by a network of hydrogen bonds and hydrophobic packing, instead of being flexible as seen in known TRPV-ARD structures. Electrophysiological recordings demonstrated that mutating key residues R225, R226, Q255, and F249 of finger 3 loop altered the channel activities and pharmacology. Taken all together, our findings show that TRPV3-ARD with characteristic finger 3 loop likely plays an important role in channel function and pharmacology.

语种: 英语
所属项目编号: 30970919 ; 81221002 ; 2013CB531300
项目资助者: National Natural Science Foundation of China ; National Basic Research Program (973 Program)
WOS记录号: WOS:000328450100011
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/59756
Appears in Collections:基础医学院_神经生物学系_期刊论文

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作者单位: 1.Peking Univ, Hlth Sci Ctr, Dept Neurobiol, Neurosci Res Inst, Beijing 100191, Peoples R China
2.Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
3.Peking Univ, Sch Pharmaceut Sci, Dept Mol & Cellular Pharmacol, State Key Lab Nat & Biomimet Drugs, Beijing 100191, Peoples R China
4.Peking Univ, PKU IDG McGovern Inst Brain Res, Beijing 100871, Peoples R China

Recommended Citation:
Shi, Di-Jing,Ye, Sheng,Cao, Xu,et al. Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for channel function[J]. PROTEIN & CELL,2013,4(12):942-950.
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