Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions

Lushpa et al report the structure and dynamics of the TLR1 toll-interleukin like (TIR) cytoplasmic domain in both crystal and solution. They demonstrate that the TLR1 TIR domain is capable of specific binding of Zn with nanomolar affinity, which appears to be critical for receptor activation, and pr...

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Autores principales: Vladislav A. Lushpa, Marina V. Goncharuk, Cong Lin, Arthur O. Zalevsky, Irina A. Talyzina, Aleksandra P. Luginina, Daniil D. Vakhrameev, Mikhail B. Shevtsov, Sergey A. Goncharuk, Alexander S. Arseniev, Valentin I. Borshchevskiy, Xiaohui Wang, Konstantin S. Mineev
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/ba1903b9028f4b788d2c7b76bc761832
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Sumario:Lushpa et al report the structure and dynamics of the TLR1 toll-interleukin like (TIR) cytoplasmic domain in both crystal and solution. They demonstrate that the TLR1 TIR domain is capable of specific binding of Zn with nanomolar affinity, which appears to be critical for receptor activation, and provide potential structures TLR1-TIR/Zn complex based on in silico data.