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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207761/
https://www.ncbi.nlm.nih.gov/pubmed/30375379
http://dx.doi.org/10.1038/s41467-018-06761-6

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207761/
https://www.ncbi.nlm.nih.gov/pubmed/30375379
http://dx.doi.org/10.1038/s41467-018-06761-6

Ejemplares similares