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Updated: Aug 30, 2025

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
Published on: September 28, 2017
HHARI in motion reveals an unexpected substrate recognition site for RBR ligases
1Department of Biochemistry, School of Biological and Behavioural Sciences, Queen Mary University of London, Blizard Institute, 4 Newark Street, London E1 2AT, UK.
Abstract:
Capturing the enzymatic activity of RBR ligases in molecular detail is challenging due to their inherent dynamic behavior. In this issue of Structure, Reiter and colleagues tackle this problem using a multidisciplinary approach. They show that activation of the ubiquitin ligase HHARI by phosphorylation induces a major conformational rearrangement, which reveals an unexpected substrate binding site.
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