Crystallization of the N-terminal domain of DFF45: The mutual chaperone   mechanism is challenged

doi:10.2174/0929866033479068

CORC > 北京大学 > 生命科学学院

	Crystallization of the N-terminal domain of DFF45: The mutual chaperone mechanism is challenged
	Li, T ; Li, X ; Yang, W ; Rao, Z ; Zhai, Z
刊名	protein and peptide letters
	2003
关键词	DFF45 DFF40 N-terminal domain crystallization chaperone DNA fragmentation apoptotic DNA FRAGMENTATION APOPTOSIS CLEAVAGE
DOI	10.2174/0929866033479068
英文摘要	DNA fragmentation factor 45 (DFF45) regulates DNase DFF40 as its inhibitor and chaperone. It was reported that the N-terminal domain (NTD) of DFF45 alone is disordered and DFF40 is necessary as a mutual chaperone for the folding of NTD. However, here we reported the crystallization of DFF45 NTD. These crystals diffract to 9Angstrom using a synchrotron radiation source. In spite of the low resolution, the demonstration of crystal formation indicates that DFF45 NTD itself is not unstructured, which strongly questions the mutual chaperone speculation about DFF45 and DFF40.; Biochemistry & Molecular Biology; SCI(E); 0; ARTICLE; 2; 221-225; 10
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/400808]
专题	生命科学学院
推荐引用方式 GB/T 7714	Li, T,Li, X,Yang, W,et al. Crystallization of the N-terminal domain of DFF45: The mutual chaperone mechanism is challenged[J]. protein and peptide letters,2003.
APA	Li, T,Li, X,Yang, W,Rao, Z,&Zhai, Z.(2003).Crystallization of the N-terminal domain of DFF45: The mutual chaperone mechanism is challenged.protein and peptide letters.
MLA	Li, T,et al."Crystallization of the N-terminal domain of DFF45: The mutual chaperone mechanism is challenged".protein and peptide letters (2003).