Gallardo, R orcid.org/0000-0003-1584-3564, Ranson, NA orcid.org/0000-0002-3640-5275 and Radford, SE orcid.org/0000-0002-3079-8039 (2020) Amyloid Structures: Much More Than Just A Cross-β Fold. Current Opinion in Structural Biology, 60. pp. 7-16. ISSN 0959-440X
Abstract
In recent years our understanding of amyloid structure has been revolutionised by innovations in cryo-electron microscopy, electron diffraction and solid-state NMR. These techniques have yielded high-resolution structures of fibrils isolated from patients with neurodegenerative disease, as well as those formed from amyloidogenic proteins in vitro. The results not only show the expected cross-β amyloid structure, but also reveal that the amyloid fold is unexpectedly diverse and complex. Here, we discuss this diversity, highlighting dynamic regions, ligand binding motifs, cavities, non-protein components, and structural polymorphism. Collectively, these variations combine to allow the generic amyloid fold to be realised in three dimensions in different ways, and this diversity may be related to the roles of fibrils in disease.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 The Author(s). Published by Elsevier Ltd. This is an open 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) > Cryo EM, Image Processing (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) |
Funding Information: | Funder Grant number Wellcome Trust 204963/Z/16/Z EU - European Union 322408 |
Depositing User: | Symplectic Publications |
Date Deposited: | 06 Sep 2019 09:09 |
Last Modified: | 13 Nov 2019 15:58 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.sbi.2019.09.001 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:150484 |