From interaction networks to interfaces, scanning intrinsically disordered regions using AlphaFold2.

ABSTRACT: The revolution brought about by AlphaFold2 opens promising perspectives to unravel the complexity of protein-protein interaction networks. The analysis of interaction networks obtained from proteomics experiments does not systematically provide the delimitations of the interaction regions. This is of particular concern in the case of interactions mediated by intrinsically disordered regions, in which the interaction site is generally small. Using a dataset of protein-peptide complexes involving intrinsically disordered regions that are non-redundant with the structures used in AlphaFold2 training, we show that when using the full sequences of the proteins, AlphaFold2-Multimer only achieves 40% success rate in identifying the correct site and structure of the interface. By delineating the i

SUBMITTER: Bret H 

PROVIDER: S-EPMC10796318 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature