Nature Communications (Oct 2018)

The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

  • Matthew G. Iadanza,
  • Robert Silvers,
  • Joshua Boardman,
  • Hugh I. Smith,
  • Theodoros K. Karamanos,
  • Galia T. Debelouchina,
  • Yongchao Su,
  • Robert G. Griffin,
  • Neil A. Ranson,
  • Sheena E. Radford

DOI
https://doi.org/10.1038/s41467-018-06761-6
Journal volume & issue
Vol. 9, no. 1
pp. 1 – 10

Abstract

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Impaired kidney function can lead to an increase of β2-microglobulin (β2m) serum levels, which can cause β2m aggregation and amyloid fibril formation. Here the authors combine cryo-EM and magic angle spinning NMR measurements to determine the structure of a β2m fibril and they also present the low resolution model of a β2m fibril with a different morphology.