New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin.
Biol Chem
; 399(8): 895-901, 2018 07 26.
Article
en En
| MEDLINE
| ID: mdl-29897879
ABSTRACT
Hydrophobins are fungal proteins that can self-assemble into amphiphilic films at hydrophobic-hydrophilic interfaces. Class I hydrophobin aggregates resemble amyloid fibrils, sharing some features with them. Here, five site-directed mutants of Vmh2, a member of basidiomycota class I hydrophobins, were designed and characterized to elucidate the molecular determinants playing a key role in class I hydrophobin self-assembly. The mechanism of fibril formation proposed for Vmh2 foresees that the triggering event is the destabilization of a specific loop (L1), leading to the formation of a ß-hairpin, which in turn generates the ß-spine of the amyloid fibril.
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Banco de datos:
MEDLINE
Asunto principal:
Proteínas Fúngicas
Idioma:
En
Año:
2018
Tipo del documento:
Article