5NAM

NMR structure of TLR4 transmembrane domain (624-670) in DMPG/DHPC bicelles

5NAM の概要

• エントリーDOI: 10.2210/pdb5nam/pdb
• NMR情報: BMRB: 34108
• 分子名称: Toll-like receptor 4 (1 entity in total)
• 機能のキーワード: toll-like receptor, protein receptor, transmembrane domain, protein, signaling 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: 5282.47

構造登録者

Mineev, K.S.,Goncharuk, S.A.,Goncharuk, M.V.,Arseniev, A.S. (登録日: 2017-02-28, 公開日: 2017-09-06, 最終更新日: 2024-06-19)

主引用文献

Mineev, K.S.,Goncharuk, S.A.,Goncharuk, M.V.,Volynsky, P.E.,Novikova, E.V.,Aresinev, A.S.
Spatial structure of TLR4 transmembrane domain in bicelles provides the insight into the receptor activation mechanism.
Sci Rep, 7:6864-6864, 2017

PubMed Abstract: Toll-like receptors (TLRs) play a key role in the innate and adaptive immune systems. While a lot of structural data is available for the extracellular and cytoplasmic domains of TLRs, and a model of the dimeric full-length TLR3 receptor in the active state was build, the conformation of the transmembrane (TM) domain and juxtamembrane regions in TLR dimers is still unclear. In the present work, we study the transmembrane and juxtamembrane parts of human TLR4 receptor using solution NMR spectroscopy in a variety of membrane mimetics, including phospholipid bicelles. We show that the juxtamembrane hydrophobic region of TLR4 includes a part of long TM α-helix. We report the dimerization interface of the TM domain and claim that long TM domains with transmembrane charged aminoacids is a common feature of human toll-like receptors. This fact is analyzed from the viewpoint of protein activation mechanism, and a model of full-length TLR4 receptor in the dimeric state has been proposed.

PubMed: 28761155
DOI: 10.1038/s41598-017-07250-4

実験手法

SOLUTION NMR