A deep learning method for predicting interactions for intrinsically disordered regions of proteins.

ABSTRACT: Intrinsically disordered proteins or regions (IDPs/IDRs) adopt diverse binding modes with different partners, ranging from ordered to multivalent to fuzzy conformations in the bound state. Characterizing IDR interfaces is challenging experimentally and computationally. Alphafold-multimer and Alphafold3, the state-of-the-art structure prediction methods, are less accurate at predicting IDR binding sites at their benchmarked confidence cutoffs. Their performance improves upon lowering the confidence cutoffs. Here, we developed Disobind, a deep-learning method that predicts inter-protein contact maps and interface residues for an IDR and a partner protein, given their sequences. It outperforms AlphaFold-multimer and AlphaFold3 at multiple confidence cutoffs. Combining the Disobind and AlphaFo

SUBMITTER: Majila K 

PROVIDER: S-EPMC11702703 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature