4OM7

Crystal structure of TIR domain of TLR6

Summary for 4OM7

• Entry DOI: 10.2210/pdb4om7/pdb
• Descriptor: Toll-like receptor 6 (2 entities in total)
• Functional Keywords: tir fold, protein interaction, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Single-pass type I membrane protein : Q9Y2C9
• Total number of polymer chains: 2
• Total formula weight: 42420.59

Authors

Park, H.H.,Jang, T.H. (deposition date: 2014-01-26, release date: 2014-08-06, Last modification date: 2024-11-27)

Primary citation

Jang, T.H.,Park, H.H.
Crystal Structure of TIR Domain of TLR6 Reveals Novel Dimeric Interface of TIR-TIR Interaction for Toll-Like Receptor Signaling Pathway.
J.Mol.Biol., 426:3305-3313, 2014

PubMed Abstract: Toll-like receptors (TLRs) are responsible for recognition of particular pathogens during the innate immune response and cytoplasmic Toll/interleukin-1 receptor (TIR) domain responsible for downstream signaling. TLR6 working with TLR2 can detect bacterial lipoprotein leading signal for nuclear factor-kappaB activation for immune response. To better understand TLR-mediated signaling event in the innate immune system, in this study, we report the first crystal structure of the TIR domain of TLR6 at 2.2Å resolution. Our structure reveals novel homo-dimerization interfaces, which might be a critical for the interaction with TIR-containing adaptor proteins and itself. We also report structural similarities and differences of TLR6 with those of other TIR domains, which may be functionally relevant.

PubMed: 25088687
DOI: 10.1016/j.jmb.2014.07.024

Experimental method

X-RAY DIFFRACTION (2.204 Å)