Haubrich, K, Spiteri, VA, Farnaby, W et al. (2 more authors) (2023) Breaking free from the crystal lattice: Structural biology in solution to study protein degraders. Current Opinion in Structural Biology, 79. 102534. ISSN 0959-440X
Abstract
Structural biology offers a versatile arsenal of techniques and methods to investigate the structure and conformational dynamics of proteins and their assemblies. The growing field of targeted protein degradation centres on the premise of developing small molecules, termed degraders, to induce proximity between an E3 ligase and a protein of interest to be signalled for degradation. This new drug modality brings with it new opportunities and challenges to structural biologists. Here we discuss how several structural biology techniques, including nuclear magnetic resonance, cryo-electron microscopy, structural mass spectrometry and small angle scattering, have been explored to complement X-ray crystallography in studying degraders and their ternary complexes. Together the studies covered in this review make a case for the invaluable perspectives that integrative structural biology techniques in solution can bring to understanding ternary complexes and designing degraders.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2023 The Authors. Published by Elsevier Ltd. This is anopen access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 24 May 2023 09:25 |
Last Modified: | 24 May 2023 09:25 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.sbi.2023.102534 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:199455 |