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@ARTICLE{Lushpa:904336,
      author       = {Lushpa, Vladislav A. and Goncharuk, Marina V. and Lin, Cong
                      and Zalevsky, Arthur O. and Talyzina, Irina A. and Luginina,
                      Aleksandra P. and Vakhrameev, Daniil D. and Shevtsov,
                      Mikhail B. and Goncharuk, Sergey A. and Arseniev, Alexander
                      S. and Borshchevskiy, Valentin and Wang, Xiaohui and Mineev,
                      Konstantin S.},
      title        = {{M}odulation of {T}oll-like receptor 1 intracellular domain
                      structure and activity by {Z}n2+ ions},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-05906},
      pages        = {1003},
      year         = {2021},
      abstract     = {Toll-like receptors (TLRs) play an important role in the
                      innate immune response. While a lot is known about the
                      structures of their extracellular parts, many questions are
                      still left unanswered, when the structural basis of TLR
                      activation is analyzed for the TLR intracellular domains.
                      Here we report the structure and dynamics of TLR1
                      toll-interleukin like (TIR) cytoplasmic domain in crystal
                      and in solution. We found that the TLR1-TIR domain is
                      capable of specific binding of Zn with nanomolar affinity.
                      Interactions with Zn are mediated by cysteine residues 667
                      and 686 and C667 is essential for the Zn binding. Potential
                      structures of the TLR1-TIR/Zn complex were predicted in
                      silico. Using the functional assays for the heterodimeric
                      TLR1/2 receptor, we found that both Zn addition and Zn
                      depletion affect the activity of TLR1, and C667A mutation
                      disrupts the receptor activity. Analysis of C667 position in
                      the TLR1 structure and possible effects of C667A mutation,
                      suggests that zinc-binding ability of TLR1-TIR domain is
                      critical for the receptor activation.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34429510},
      UT           = {WOS:000688061400003},
      doi          = {10.1038/s42003-021-02532-0},
      url          = {https://juser.fz-juelich.de/record/904336},
}