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8AR3

Solution structure of TLR9 transmembrane and cytoplasmic juxtamembrane regions

8AR3 の概要
エントリーDOI10.2210/pdb8ar3/pdb
NMR情報BMRB: 34753
分子名称Toll-like receptor 9 (1 entity in total)
機能のキーワードprotein, membrane protein
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計5805.93
構造登録者
Kornilov, F.D.,Shabalkina, A.V.,Goncharuk, M.V.,Goncharuk, S.A.,Arseniev, A.S.,Mineev, K.S. (登録日: 2022-08-15, 公開日: 2023-03-22, 最終更新日: 2024-06-19)
主引用文献Kornilov, F.D.,Shabalkina, A.V.,Lin, C.,Volynsky, P.E.,Kot, E.F.,Kayushin, A.L.,Lushpa, V.A.,Goncharuk, M.V.,Arseniev, A.S.,Goncharuk, S.A.,Wang, X.,Mineev, K.S.
The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors.
Nat Commun, 14:1503-1503, 2023
Cited by
PubMed Abstract: Toll-like receptors (TLRs) are the important participants of the innate immune response. Their spatial organization is well studied for the ligand-binding domains, while a lot of questions remain unanswered for the membrane and cytoplasmic regions of the proteins. Here we use solution NMR spectroscopy and computer simulations to investigate the spatial structures of transmembrane and cytoplasmic juxtamembrane regions of TLR2, TLR3, TLR5, and TLR9. According to our data, all the proteins reveal the presence of a previously unreported structural element, the cytoplasmic hydrophobic juxtamembrane α-helix. As indicated by the functional tests in living cells and bioinformatic analysis, this helix is important for receptor activation and plays a role, more complicated than a linker, connecting the transmembrane and cytoplasmic parts of the proteins.
PubMed: 36932058
DOI: 10.1038/s41467-023-37042-6
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 8ar3
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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