ArticleBiophysical journal2023
Template-free prediction of a new monotopic membrane protein fold and assembly by AlphaFold2.
Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026Review
- Phosphorylation-dependent structure and dynamics of caveolin-1 8S complex.Biophysical journal · 2026Article
- Evolutionarily diverse caveolins share a common structural framework built around amphipathic disks.The Journal of cell biology · 2025Article
- Hybrid framework for membrane protein type prediction based on the PSSM.Scientific reports · 2024Article
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- Computational drug development for membrane protein targets.Nature biotechnology · 2024Review
- Simulations suggest a scaffolding mechanism of membrane deformation by the caveolin 8S complex.Biophysical journal · 2023Article
- Membranes in focus.Biophysical journal · 2023Article
- The building blocks of caveolae revealed: caveolins finally take center stage.Biochemical Society transactions · 2023Article
- Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.Nature communications · 2023Article
- Benchmarking AlphaFold2 on peptide structure prediction.Structure (London, England : 1993) · 2023Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
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 the interfaces between them. It also assembles between seven 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.