Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets

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

doi:10.1038/ncomms15540

Nature Communications (Jun 2017)

Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets

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

Affiliations

Xiuxiu Lu: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
Urszula Nowicka: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
Vinidhra Sridharan: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
Fen Liu: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
Leah Randles: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
David Hymel: Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute
Marzena Dyba: Basic Science Program, Leidos Biomedical Research, Inc., Structural Biophysics Laboratory, Frederick National Lab
Sergey G. Tarasov: Biophysics Resource, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute
Nadya I. Tarasova: Cancer and Inflammation Program, Center for Cancer Research, National Cancer Institute
Xue Zhi Zhao: Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute
Jun Hamazaki: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, University of Tokyo
Shigeo Murata: Laboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, University of Tokyo
Terrence R. Burke, Jr.: Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute
Kylie J. Walters: Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute

DOI: https://doi.org/10.1038/ncomms15540
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 13

Abstract

Read online

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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal