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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, ? = 118.89°

SUBMITTER: Jang TH

PROVIDER: S-EPMC4118802 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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

Jang Tae-ho TH Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology communications 20140723 Pt 8

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 belon ...[more]

PMID: 25084380

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