Expression, purification, and co-crystallization of IRF-I bound to the interferon-beta element PRDI

被引:12
作者
Escalante, CR
Yie, JM
Thanos, D
Aggarwal, AK
机构
[1] MT SINAI SCH MED,STRUCT BIOL PROGRAM,DEPT PHYSIOL & BIOPHYS,NEW YORK,NY 10029
[2] COLUMBIA UNIV,COLL PHYS & SURG,DEPT BIOCHEM & MOL BIOPHYS,NEW YORK,NY 10032
关键词
X-ray crystallography; interferon; transcription factor; DNA-binding protein;
D O I
10.1016/S0014-5793(97)00996-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Interferon regulatory factor 1 (IRF-1) is an essential factor involved in the regulation of type I interferon (IFN) and IFN-inducible genes, The protein consists of 329 amino acids that are highly conserved from mouse to human, Similar to other transcription factors, the protein is modular in nature with a basic N-terminal region involved in DNA binding and an acidic C-terminal region required for activation, We report here the expression, purification and co-crystallization of the minimal N-terminal region of IRF-1 involved in DNA binding (amino acids 1-113) with a 13 bp DNA fragment from the IFN-beta promoter, The crystals diffract to at least 3.0 Angstrom in resolution and belong to space group R3 with unit cell parameters of a=b=84.8 Angstrom, c = 203.7 Angstrom. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:219 / 220
页数:2
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