Structure determination of human Fas apoptosis inhibitory molecule and identification of the critical residues linking the interdomain interaction to the anti-apoptotic activity
- 影响因子：
0.0
- 发表刊物：
Acta Crystallogr D Biol Crystallogr
- 关键字：
Fas apoptosis inhibitory molecule; anti-apoptotic protein; interdomain interaction
- 摘要：
Fas apoptosis inhibitory molecule (FAIM) is a highly conserved anti-apoptotic protein which plays important roles in cells. There are two isoforms of FAIM, of which the short isoform FAIM-S is broadly expressed in all tissues, whereas the long isoform FAIM-L is exclusively expressed in the nervous system. No structure of human FAIM has been reported to date and the detailed molecular mechanisms underlying the anti-apoptotic function of FAIM remain unknown. Here, the crystal structure of the human FAIM-S N-terminal domain (NTD) and the NMR solution structure of the human FAIM-S C-terminal domain (CTD) were determined. The structures revealed that the NTD and CTD adopt a similar protein fold containing eight antiparallel β-strands which form two sheets. Both structural and biochemical analyses implied that the NTD exists as a dimer and the CTD as a monomer and that they can interact with each other. Several critical residues were identified to be involved in this interaction. Moreover, mutations of these critical residues also interfered in the anti-apoptotic activity of FAIM-S. Thus, the structural and functional data presented here will provide insight into the anti-apoptotic mechanism of FAIM-S.
- 论文类型：
期刊论文
- 论文编号：
43
- 卷号：
70
- 期号：
7
- 页面范围：
1812-1822
- 是否译文：
否
- 发表时间：
2014-07-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Li Guoming
- 通讯作者：
Jin Changwen,Zheng Xiaofeng
- 全部作者：
Qu Linglong,Ma Shuaipeng,Wu Yujie
