Liu Dongsheng, Feng Yingang, Cheng Yuan, Wang Jinfeng
National Laboratory of Biomacromolecules, Center for Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.
Biochem Biophys Res Commun. 2004 May 28;318(2):391-6. doi: 10.1016/j.bbrc.2004.04.044.
Programmed cell death 5 (PDCD5) protein is phylogenetically conserved in both the nucleus and cytoplasm. The human PDCD5 protein is expressed in tumor cells during apoptosis independent of the apoptosis-inducing stimuli, and recently it was found that PDCD5 is an important regulator in both apoptotic and non-apoptotic programmed cell death. In this study, human PDCD5 was expressed in Escherichia coli cell and studied using heteronuclear NMR method. The NMR results indicate that PDCD5 protein can be divided into three structural regions, a core region and two dissociated terminal regions. The core region (41-101) represents a rigid sub-domain consisting mainly of a triple-helix bundle. The N-terminal 38 residues (3-40) are ordered, but not a rigid structural region which contains abundant secondary structure, and packs very loosely against the core. The C-terminal 17 residues (102-118) represent a mobile unstructured region, which may be capable of interaction with nucleic acid.
程序性细胞死亡蛋白5（PDCD5）在细胞核和细胞质中均具有系统发育保守性。人PDCD5蛋白在肿瘤细胞凋亡过程中表达，与凋亡诱导刺激无关，最近发现PDCD5在凋亡性和非凋亡性程序性细胞死亡中均为重要调节因子。在本研究中，人PDCD5在大肠杆菌细胞中表达，并采用异核核磁共振方法进行研究。核磁共振结果表明，PDCD5蛋白可分为三个结构区域，一个核心区域和两个解离的末端区域。核心区域（41-101）代表一个刚性亚结构域，主要由一个三螺旋束组成。N端的38个残基（3-40）有序排列，但不是一个刚性结构区域，该区域含有丰富的二级结构，并且与核心区域的堆积非常松散。C端的17个残基（102-118）代表一个可移动的无结构区域，可能能够与核酸相互作用。
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