High-throughput assay exploiting disorder-to-order conformational switches: application to the proteasomal Rpn10:E6AP complex-Reference-Cited by-同舟云学术

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High-throughput assay exploiting disorder-to-order conformational switches: application to the proteasomal Rpn10:E6AP complex

Published:2024 Issue:11 Volume:15 Page:4041-4053
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Muli Christine S.¹^ORCID,Tarasov Sergey G.²^ORCID,Walters Kylie J.¹^ORCID

Affiliation:

1. Protein Processing Section, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, 21702, USA

2. Biophysics Resource, Center for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA

Abstract

An assay was developed to monitor a disorder-to-order switch in proteasome subunit Rpn10 that is induced by E6AP binding. Fluorophores acrylodan and Atto610 differentially measured E6AP-induced helicity in Rpn10 RAZUL, allowing for dual application.

Funder

National Cancer Institute

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D3SC06370D

Reference72 articles.

1. An expanded lexicon for the ubiquitin code

2. Proteasome substrate receptors and their therapeutic potential

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4. Degradation of proteins by PROTACs and other strategies

5. Proteolysis targeting chimera (PROTAC) in drug discovery paradigm: Recent progress and future challenges

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