PPIscreenML is a method for structure-based screening of protein-protein interactions using AlphaFold

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Authors: Victoria Mischley, Johannes Maier, Jesse Chen, John Karanicolas
Cited by: 1
References: 48

Abstract

Protein-protein interactions underlie nearly all cellular processes. With the advent of protein structure prediction methods such as AlphaFold2 (AF2), models of specific protein pairs can be built extremely accurately in most cases. However, determining the relevance of a given protein pair remains an open question. It is presently unclear how to use best structure-based tools to infer whether a pair of candidate proteins indeed interacts with one another: ideally, one might even use such information to screen among candidate pairings to build up protein interaction networks. Whereas methods for evaluating quality of modeled protein complexes have been co-opted for determining which pairings interact (e.g. pDockQ and iPTM), there have been no rigorously benchmarked methods for this task. Here, we introduce PPIscreenML, a classification model trained to distinguish AF2 models of interacting protein pairs from AF2 models of compelling decoy pairings. We find that PPIscreenML outperforms methods such as pDockQ and iPTM for this task, and further that PPIscreenML exhibits impressive performance when identifying which ligand/receptor pairings engage one another across the structurally conserved tumor necrosis factor superfamily (TNFSF). Analysis of benchmark results using complexes not seen in PPIscreenML development strongly suggests that the model generalizes beyond training data, making it broadly applicable for identifying new protein complexes based on structural models built with AF2.

Fields of Study & Subjects

Bioinformatics and Genomic Networks Protein Structure and Dynamics Biomedical Text Mining and Ontologies

Publication details

Journal / source
eLife
Publisher
eLife Sciences Publications, Ltd
Volume
13
Publication date
21 April 2026
Language
EN