PPI-hotspot^ID for detecting protein-protein interaction hot spots from the free protein structure.

ABSTRACT: Experimental detection of residues critical for protein-protein interactions (PPI) is a time-consuming, costly, and labor-intensive process. Hence, high-throughput PPI-hot spot prediction methods have been developed, but they have been validated using relatively small datasets, which may compromise their predictive reliability. Here, we introduce PPI-hotspot^ID, a novel method for identifying PPI-hot spots using the free protein structure, and validated it on the largest collection of experimentally confirmed PPI-hot spots to date. We explored the possibility of detecting PPI-hot spots using (i) FTMap in the PPI mode, which identifies hot spots on protein-protein interfaces from the free protein structure, and (ii) the interface residues predicted by AlphaFold-Multimer. PP

SUBMITTER: Chen YC 

PROVIDER: S-EPMC11405013 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature