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The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors

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  • F. D. Kornilov

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

  • A. V. Shabalkina

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

  • Cong Lin

    (Chinese Academy of Sciences)

  • P. E. Volynsky

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Institute of Cytology of Russian Academy of Sciences)

  • E. F. Kot

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

  • A. L. Kayushin

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry)

  • V. A. Lushpa

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

  • M. V. Goncharuk

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry)

  • A. S. Arseniev

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry)

  • S. A. Goncharuk

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

  • Xiaohui Wang

    (Chinese Academy of Sciences
    University of Science and Technology of China)

  • K. S. Mineev

    (Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry
    Moscow Institute of Physics and Technology)

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.

Suggested Citation

  • F. D. Kornilov & A. V. Shabalkina & Cong Lin & P. E. Volynsky & E. F. Kot & A. L. Kayushin & V. A. Lushpa & M. V. Goncharuk & A. S. Arseniev & S. A. Goncharuk & Xiaohui Wang & K. S. Mineev, 2023. "The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37042-6
    DOI: 10.1038/s41467-023-37042-6
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    References listed on IDEAS

    as
    1. Beom Seok Park & Dong Hyun Song & Ho Min Kim & Byong-Seok Choi & Hayyoung Lee & Jie-Oh Lee, 2009. "The structural basis of lipopolysaccharide recognition by the TLR4–MD-2 complex," Nature, Nature, vol. 458(7242), pages 1191-1195, April.
    2. Yingwu Xu & Xiao Tao & Baohe Shen & Tiffany Horng & Ruslan Medzhitov & James L. Manley & Liang Tong, 2000. "Structural basis for signal transduction by the Toll/interleukin-1 receptor domains," Nature, Nature, vol. 408(6808), pages 111-115, November.
    3. Umeharu Ohto & Takuma Shibata & Hiromi Tanji & Hanako Ishida & Elena Krayukhina & Susumu Uchiyama & Kensuke Miyake & Toshiyuki Shimizu, 2015. "Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9," Nature, Nature, vol. 520(7549), pages 702-705, April.
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