The structure of a β(2)-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear. Here, we combine cryo-EM and MAS-NMR to determine the structure of an amyloid fibril formed in vitro from β(2)-microglobulin (β(2)m), the culprit...

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Bibliografische gegevens
Gepubliceerd in:Nat Commun
Hoofdauteurs: Iadanza, Matthew G., Silvers, Robert, Boardman, Joshua, Smith, Hugh I., Karamanos, Theodoros K., Debelouchina, Galia T., Su, Yongchao, Griffin, Robert G., Ranson, Neil A., Radford, Sheena E.
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Nature Publishing Group UK 2018
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Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC6207761/
https://ncbi.nlm.nih.gov/pubmed/30375379
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-018-06761-6
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