title: Preliminary X-ray crystallographic studies of the TIR domain of human Toll-like receptor 6.
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°C. Finally, X-ray diffraction data were collected to a resolution of 2.2 Å from a crystal belonging to space group C2, with unit-cell parameters a = 127.60, b = 44.20, c = 75.72 Å, β = 118.89°
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Tae-ho
authors.initials: TH
authors.lastname: Jang
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D001483:Base Sequence; D018360:Crystallography, X-Ray; D017931:DNA Primers; D006801:Humans; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D051216:Toll-Like Receptor 6 / Q000737:chemistry*
chemical_list: D017931:DNA Primers; C495368:TLR6 protein, human; D051216:Toll-Like Receptor 6
keywords: TIR domain; Toll-like receptor 6
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