Preliminary X-ray crystallographic studies of the TIR domain of human Toll-like receptor 6

被引:2
作者
Jang, Tae-Ho
Park, Hyun Ho [1 ]
机构
[1] Yeungnam Univ, Sch Biotechnol, Gyongsan, South Korea
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷
基金
新加坡国家研究基金会;
关键词
CRYSTAL-STRUCTURE; PROTEIN;
D O I
10.1107/S2053230X1401245X
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Toll-like receptor (TLR) proteins have been identified and shown to play a role in the innate immune response. TLR6 associated with TLR2 can recognize diacylated lipoprotein. In this study, the human TLR6 TIR domain corresponding to amino acids 640-796 was overexpressed in Escherichia coli using engineered C-terminal His tags. The TLR6 TIR domain was then purified to homogeneity and crystallized at 20 degrees C. Finally, X-ray diffraction data were collected to a resolution of 2.2 angstrom from a crystal belonging to space group C2, with unit-cell parameters a = 127.60, b = 44.20, c = 75.72 angstrom beta = 118.89 degrees
引用
收藏
页码:1053 / 1055
页数:3
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