Computational design and molecular dynamics simulations suggest the mode of substrate binding in ceramide synthases.
Nat Commun
; 14(1): 2330, 2023 04 22.
Article
em En
| MEDLINE
| ID: mdl-37087500
ABSTRACT
Until now, membrane-protein stabilization has relied on iterations of mutations and screening. We now validate a one-step algorithm, mPROSS, for stabilizing membrane proteins directly from an AlphaFold2 model structure. Applied to the lipid-generating enzyme, ceramide synthase, 37 designed mutations lead to a more stable form of human CerS2. Together with molecular dynamics simulations, we propose a pathway by which substrates might be delivered to the ceramide synthases.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ceramidas
/
Simulação de Dinâmica Molecular
Limite:
Humans
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article