Back

Improving AlphaFold 3 structural modeling by incorporating explicit crosslinks

Kosinski, J.

2024-12-03 molecular biology
10.1101/2024.12.03.626671 bioRxiv
Show abstract

AlphaFold 3 has significantly advanced the modeling of macromolecular structures, including proteins, DNA, RNA, and their interactions with small molecules or post-translational modifications. However, challenges remain when modeling specific structural conformations or complexes with limited evolutionary data, such as protein-antibody complexes. Previous studies with AlphaFold2 demonstrated that adding distance restraints from crosslinking mass spectrometry (XL-MS) can improve predictions for such cases. In this study, we investigate whether XL-MS restraints can be incorporated into AlphaFold 3 by explicitly modeling crosslinks as covalently-bound ligands. Our results show that this approach is able to increase the accuracy of AlphaFold 3 models. We explore the opportunities and limitations of this method, which has been implemented as a proof-of-concept pipeline named AF3x, available at https://github.com/KosinskiLab/af3x.

Matching journals

The top 5 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.