Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets
In the proteasome, Rpn2 provides the docking site for substrate receptor Rpn13. Here the authors present the structure of human Rpn13 Pru domain bound to its binding site in Rpn2 and provide insights into the mode of action for Rpn13-targeting molecule RA190, which has anticancer properties.
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Nature Portfolio
2017
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oai:doaj.org-article:3558b297c27d4dde9ca8b170d554b63a2021-12-02T14:42:20ZStructure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets10.1038/ncomms155402041-1723https://doaj.org/article/3558b297c27d4dde9ca8b170d554b63a2017-06-01T00:00:00Zhttps://doi.org/10.1038/ncomms15540https://doaj.org/toc/2041-1723In the proteasome, Rpn2 provides the docking site for substrate receptor Rpn13. Here the authors present the structure of human Rpn13 Pru domain bound to its binding site in Rpn2 and provide insights into the mode of action for Rpn13-targeting molecule RA190, which has anticancer properties.Xiuxiu LuUrszula NowickaVinidhra SridharanFen LiuLeah RandlesDavid HymelMarzena DybaSergey G. TarasovNadya I. TarasovaXue Zhi ZhaoJun HamazakiShigeo MurataTerrence R. Burke, Jr.Kylie J. WaltersNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017) |
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Science Q |
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Science Q Xiuxiu Lu Urszula Nowicka Vinidhra Sridharan Fen Liu Leah Randles David Hymel Marzena Dyba Sergey G. Tarasov Nadya I. Tarasova Xue Zhi Zhao Jun Hamazaki Shigeo Murata Terrence R. Burke, Jr. Kylie J. Walters Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
description |
In the proteasome, Rpn2 provides the docking site for substrate receptor Rpn13. Here the authors present the structure of human Rpn13 Pru domain bound to its binding site in Rpn2 and provide insights into the mode of action for Rpn13-targeting molecule RA190, which has anticancer properties. |
format |
article |
author |
Xiuxiu Lu Urszula Nowicka Vinidhra Sridharan Fen Liu Leah Randles David Hymel Marzena Dyba Sergey G. Tarasov Nadya I. Tarasova Xue Zhi Zhao Jun Hamazaki Shigeo Murata Terrence R. Burke, Jr. Kylie J. Walters |
author_facet |
Xiuxiu Lu Urszula Nowicka Vinidhra Sridharan Fen Liu Leah Randles David Hymel Marzena Dyba Sergey G. Tarasov Nadya I. Tarasova Xue Zhi Zhao Jun Hamazaki Shigeo Murata Terrence R. Burke, Jr. Kylie J. Walters |
author_sort |
Xiuxiu Lu |
title |
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
title_short |
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
title_full |
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
title_fullStr |
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
title_full_unstemmed |
Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets |
title_sort |
structure of the rpn13-rpn2 complex provides insights for rpn13 and uch37 as anticancer targets |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/3558b297c27d4dde9ca8b170d554b63a |
work_keys_str_mv |
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