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- W4288710679 abstract "Abstract The VPS13 protein family constitutes a novel class of bridge-like lipid transferases. Autosomal recessive inheritance of mutations in VPS13 genes is associated with the development of neurodegenerative diseases in humans. Bioinformatic approaches previously recognised the domain architecture of these proteins. In this study, we model the first ever full-length structures of the four human homologs VPS13A, VPS13B, VPS13C, and VPS13D in association with model membranes, to investigate their lipid transfer ability and potential structural association with membrane leaflets. We analyse the evolutionary conservation and physicochemical properties of these proteins, focusing on conserved C-terminal amphipathic helices that disturb organelle surfaces and that, adjoined, resemble a traditional Venetian gondola. The gondola domains share significant structural homology with lipid droplet surface-binding proteins. We introduce in silico protein-membrane models displaying the mode of association of VPS13A, VPS13B, VPS13C, and VPS13D to donor and target membranes, and present potential models of action for protein-mediated lipid transfer." @default.
- W4288710679 created "2022-07-30" @default.
- W4288710679 creator A5062844651 @default.
- W4288710679 creator A5073806326 @default.
- W4288710679 creator A5088452021 @default.
- W4288710679 date "2022-07-29" @default.
- W4288710679 modified "2023-10-16" @default.
- W4288710679 title "<i>In silico</i> modelling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanisms" @default.
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