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

The structure of a β2-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 β2-microglobulin (β2m), the culprit pro...

Full description

Bibliographic Details
Main Authors: Iadanza, Matthew G. (Author), Boardman, Joshua (Author), Smith, Hugh I. (Author), Karamanos, Theodoros K. (Author), Ranson, Neil A. (Author), Radford, Sheena E. (Author), Silvers, Robert Paul Georg (Contributor), Debelouchina, Galia Tzvetanova (Contributor), Su, Yongchao (Contributor), Griffin, Robert Guy (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor), Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology) (Contributor)
Format: Article
Language:English
Published: Nature Publishing Group, 2019-03-07T15:23:07Z.
Subjects:
Article
Online Access:Get fulltext

Internet

Get fulltext

Similar Items