7YLG

Crystal structure of the chicken Toll-like receptor 15 TIR domain (glutathione adduct)

7YLG の概要

• エントリーDOI: 10.2210/pdb7ylg/pdb
• 分子名称: Toll-like receptor 2, GLUTATHIONE (3 entities in total)
• 機能のキーワード: innate immune receptor, immune system
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21044.00

構造登録者

Ko, K.Y.,Song, W.S.,Yoon, S.I. (登録日: 2022-07-26, 公開日: 2023-05-31, 最終更新日: 2023-11-29)

主引用文献

Ko, K.Y.,Song, W.S.,Park, J.,Lee, G.S.,Yoon, S.I.
Structural analysis of the Toll-like receptor 15 TIR domain.
Iucrj, 10:352-362, 2023

PubMed Abstract: Toll-like receptors (TLRs) activate innate immunity in response to pathogen-associated molecular patterns (PAMPs). The ectodomain of a TLR directly senses a PAMP and the intracellular TIR domain dimerizes to initiate a signaling cascade. The TIR domains of TLR6 and TLR10, which belong to the TLR1 subfamily, have been structurally characterized in a dimer, whereas those of other subfamilies, including TLR15, have not been explored at the structural or molecular level. TLR15 is a TLR unique to birds and reptiles that responds to virulence-associated fungal and bacterial proteases. To reveal how the TLR15 TIR domain (TLR15) triggers signaling, the crystal structure of TLR15 was determined in a dimeric form and a mutational study was performed. TLR15 forms a one-domain structure in which a five-stranded β-sheet is decorated by α-helices, as shown for TLR1 subfamily members. TLR15 exhibits substantial structural differences from other TLRs at the BB and DD loops and αC2 helix that are involved in dimerization. As a result, TLR15 is likely to form a dimeric structure that is unique in its intersubunit orientation and the contribution of each dimerizing region. Further comparative analysis of TIR structures and sequences provides insights into the recruitment of a signaling adaptor protein by TLR15.

PubMed: 37079400
DOI: 10.1107/S2052252523002956

実験手法

X-RAY DIFFRACTION (1.8 Å)