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
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/ba1903b9028f4b788d2c7b76bc761832
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spelling oai:doaj.org-article:ba1903b9028f4b788d2c7b76bc7618322021-12-02T19:02:27ZModulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions10.1038/s42003-021-02532-02399-3642https://doaj.org/article/ba1903b9028f4b788d2c7b76bc7618322021-08-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-02532-0https://doaj.org/toc/2399-3642Lushpa 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.Vladislav A. LushpaMarina V. GoncharukCong LinArthur O. ZalevskyIrina A. TalyzinaAleksandra P. LugininaDaniil D. VakhrameevMikhail B. ShevtsovSergey A. GoncharukAlexander S. ArsenievValentin I. BorshchevskiyXiaohui WangKonstantin S. MineevNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Biology (General)
QH301-705.5
spellingShingle Biology (General)
QH301-705.5
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
Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
description 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.
format article
author 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
author_facet 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
author_sort Vladislav A. Lushpa
title Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
title_short Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
title_full Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
title_fullStr Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
title_full_unstemmed Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn2+ ions
title_sort modulation of toll-like receptor 1 intracellular domain structure and activity by zn2+ ions
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/ba1903b9028f4b788d2c7b76bc761832
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