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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2021
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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) |
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DOAJ |
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Biology (General) QH301-705.5 |
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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 |
work_keys_str_mv |
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