An atlas of protein homo-oligomerization across domains of life

This is a little outside of "ML for Omics" other than it being proteomics-related.

They scaled AlphaFold2 predictions for possible homodimers across P. furiosus, E. coli, S. cerevisiae, and H. sapiens proteomes (20-45%), analyzing those with physiological relevance and processed those into higher-order structures. The result: gorgeous structures.

They actually validated one of the predicted large structures by cryo-EM as well, showing that at least some of their predictions are reasonable.

Takeaways:

  • coiled-coil regions are major drivers of quaternary structure

  • interaction interfaces in homo-oligomers are ~70% more likely to contain disease mutations than protein surfaces

  • lots of these complexes appear to be symmetric.

https://www.cell.com/cell/pdf/S0092-8674(24)00059-X.pdf

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