3J0A

Homology model of human Toll-like receptor 5 fitted into an electron microscopy single particle reconstruction

3J0A の概要

• エントリーDOI: 10.2210/pdb3j0a/pdb
• EMDBエントリー: 5287 5288
• 分子名称: Toll-like receptor 5, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: toll-like receptor 5, membrane protein, leucine-rich repeat, asymmetric homodimer, glycoprotein, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 198455.62

構造登録者

Modis, Y.,Zhou, K.,Kanai, R.,Lee, P.,Wang, H.W. (登録日: 2011-06-02, 公開日: 2011-12-28, 最終更新日: 2024-11-20)

主引用文献

Zhou, K.,Kanai, R.,Lee, P.,Wang, H.W.,Modis, Y.
Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin.
J.Struct.Biol., 177:402-409, 2012

PubMed Abstract: The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions. The structure shows that like TLR9, TLR5 dimerizes in the absence of ligand. The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold. A TLR5 homology model was generated and fitted into the electron microscopy structure. All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface. Glycosylation at the first five sites was confirmed by tandem mass spectrometry. Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342. In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans. Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.

PubMed: 22173220
DOI: 10.1016/j.jsb.2011.12.002

実験手法

ELECTRON MICROSCOPY (26 Å)