Structure prediction of novel isoforms from uveal melanoma by AlphaFold

Alternative splicing is an important mechanism that enhances protein functional diversity. To date, our understanding of alternative splicing variants has been based on mRNA transcript data, but due to the difficulty in predicting protein structures, protein tertiary structures have been largely unexplored. However, with the release of AlphaFold, which predicts three-dimensional models of proteins, this challenge is rapidly being overcome. Here, we present a dataset of 315 predicted structures of abnormal isoforms in 18 uveal melanoma patients based on second- and third-generation transcriptome-sequencing data. This information comprises a high-quality set of structural data on recurrent aberrant isoforms that can be used in multiple types of studies, from those aimed at revealing potential therapeutic targets to those aimed at recognizing of cancer neoantigens at the atomic level.

Automated summary

Alternative splicing is an important mechanism for protein diversity, but our understanding of protein structures has been limited. However, the release of AlphaFold has allowed for the prediction of protein structures, enabling the exploration of abnormal isoforms in uveal melanoma patients. This dataset provides valuable structural information for studying potential therapeutic targets and cancer neoantigens at an atomic level.