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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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| Pubblicato in: | Nat Commun |
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| Autori principali: | , , , , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group UK
2018
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| Soggetti: | |
| Accesso online: | 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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