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- W4285087160 abstract "Abstract AlphaFold2 (AF2) has revolutionized the field of protein structural prediction. Here, we test its ability to predict the tertiary and quaternary structure of a previously undescribed scaffold with new folds and unusual architecture, the monotopic membrane protein caveolin-1 (CAV1). CAV1 assembles into a disc-shaped oligomer composed of 11 symmetrically arranged protomers, each assuming an identical new fold, and contains the largest parallel β-barrel known to exist in nature. Remarkably, AF2 predicts both the fold of the protomers and interfaces between them. It also assembles between 7 and 15 copies of CAV1 into disc-shaped complexes. However, the predicted multimers are energetically strained, especially the parallel β-barrel. These findings highlight the ability of AF2 to correctly predict new protein folds and oligomeric assemblies at a granular level while missing some elements of higher order complexes, thus positing a new direction for the continued development of deep learning protein structure prediction approaches." @default.
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- W4285087160 date "2022-07-13" @default.
- W4285087160 modified "2023-10-06" @default.
- W4285087160 title "Template-free prediction of a new monotopic membrane protein fold and oligomeric assembly by Alphafold2" @default.
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- W4285087160 doi "https://doi.org/10.1101/2022.07.12.499809" @default.
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