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

Title
Preliminary X-ray crystallographic studies of the TIR domain of human Toll-like receptor 6
Author(s)
박현호장태호
Keywords
CRYSTAL-STRUCTURE; PROTEIN
Issue Date
201408
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.1053 - 1055
Abstract
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
URI
http://hdl.handle.net/YU.REPOSITORY/31220http://dx.doi.org/10.1107/S2053230X1401245X
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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