Disease-relevant β2-microglobulin variants share a common amyloid fold

The authors use cryo-EM to determine amyloid fibrils structures of disease relevant variants of β2-microglobulin in vitro. Each variant is polymorphic, but all polymorphs from all samples are built from a a lego-like assembly of common building blocks, suggesting a one amyloid fold’ paradigm.

Bibliographic Details
Main Authors: Martin Wilkinson, Rodrigo U. Gallardo, Roberto Maya Martinez, Nicolas Guthertz, Masatomo So, Liam D. Aubrey, Sheena E. Radford, Neil A. Ranson
Format: Article
Language:English
Published: Nature Portfolio 2023-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-023-36791-8
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author Martin Wilkinson
Rodrigo U. Gallardo
Roberto Maya Martinez
Nicolas Guthertz
Masatomo So
Liam D. Aubrey
Sheena E. Radford
Neil A. Ranson
author_facet Martin Wilkinson
Rodrigo U. Gallardo
Roberto Maya Martinez
Nicolas Guthertz
Masatomo So
Liam D. Aubrey
Sheena E. Radford
Neil A. Ranson
author_sort Martin Wilkinson
collection DOAJ
description The authors use cryo-EM to determine amyloid fibrils structures of disease relevant variants of β2-microglobulin in vitro. Each variant is polymorphic, but all polymorphs from all samples are built from a a lego-like assembly of common building blocks, suggesting a one amyloid fold’ paradigm.
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spelling doaj.art-e2de69dabe954fc29c63847d4f346f102023-03-22T11:41:41ZengNature PortfolioNature Communications2041-17232023-03-0114111510.1038/s41467-023-36791-8Disease-relevant β2-microglobulin variants share a common amyloid foldMartin Wilkinson0Rodrigo U. Gallardo1Roberto Maya Martinez2Nicolas Guthertz3Masatomo So4Liam D. Aubrey5Sheena E. Radford6Neil A. Ranson7Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of LeedsThe authors use cryo-EM to determine amyloid fibrils structures of disease relevant variants of β2-microglobulin in vitro. Each variant is polymorphic, but all polymorphs from all samples are built from a a lego-like assembly of common building blocks, suggesting a one amyloid fold’ paradigm.https://doi.org/10.1038/s41467-023-36791-8
spellingShingle Martin Wilkinson
Rodrigo U. Gallardo
Roberto Maya Martinez
Nicolas Guthertz
Masatomo So
Liam D. Aubrey
Sheena E. Radford
Neil A. Ranson
Disease-relevant β2-microglobulin variants share a common amyloid fold
Nature Communications
title Disease-relevant β2-microglobulin variants share a common amyloid fold
title_full Disease-relevant β2-microglobulin variants share a common amyloid fold
title_fullStr Disease-relevant β2-microglobulin variants share a common amyloid fold
title_full_unstemmed Disease-relevant β2-microglobulin variants share a common amyloid fold
title_short Disease-relevant β2-microglobulin variants share a common amyloid fold
title_sort disease relevant β2 microglobulin variants share a common amyloid fold
url https://doi.org/10.1038/s41467-023-36791-8
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