Spatial structure of TLR4 transmembrane domain in bicelles provides the insight into the receptor activation mechanism

• Published in: Scientific reports Vol. 7; no. 1; pp. 6864 - 12
• Main Authors: Mineev, Konstantin S., Goncharuk, Sergey A., Goncharuk, Marina V., Volynsky, Pavel E., Novikova, Ekaterina V., Aresinev, Alexander S.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 31.07.2017; Nature Publishing Group; Nature Portfolio
• Subjects: 101/6; 631/45/612/1237; 631/535/878/1263; 64; 82; 82/16; 82/29; 82/6; 82/80; 82/83; Dimerization; Humanities and Social Sciences; Hydrophobicity; Investigations; Ligands; Lipids; Magnetic resonance spectroscopy; multidisciplinary; NMR; Nuclear magnetic resonance; Peptides; Phospholipids; Polymorphism; Protein structure; Proteins; Receptor mechanisms; Science; Science (multidisciplinary); Spectroscopy; TLR3 protein; TLR4 protein; Toll-like receptors; Transmembrane domains

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 transme...