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Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUS

Protein domains without the usual distribution of amino acids, called low complexity (LC) domains, can be prone to self-assembly into amyloid-like fibrils. Self-assembly of LC domains that are nearly devoid of hydrophobic residues, such as the 214-residue LC domain of the RNA-binding protein FUS, is...

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Publicat a:Nat Commun
Autors principals: Lee, Myungwoon, Ghosh, Ujjayini, Thurber, Kent R., Kato, Masato, Tycko, Robert
Format: Artigo
Idioma:Inglês
Publicat: Nature Publishing Group UK 2020
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC7665218/
https://ncbi.nlm.nih.gov/pubmed/33184287
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41467-020-19512-3
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