Assessment of scoring functions for computational models of protein-protein interfaces.

An important goal of computational studies of protein-protein interfaces (PPIs) is to predict the binding site between two monomers that form a heterodimer. The simplest version of this problem is to rigidly re-dock the bound forms of the monomers, which involves generating computational models of the heterodimer and then scoring them to determine the most native-like models. PPI scoring functions have been assessed previously using rank- and classification-based metrics; however, these methods are sensitive to the number and quality of models in the scoring function training set. We assess the accuracy of seven PPI scoring functions by comparing their scores of computational models of PPIs to a measure of structural similarity to the x-ray crystal structure (i.e. the DockQ score) for a non-redundant set of heterodimers from the Protein Data Bank. For each heterodimer, we generate re-docked models uniformly sampled over DockQ and calculate the Spearman correlation between the PPI scores and DockQ. For some targets, the scores and DockQ are highly correlated; however, for many targets, there are weak correlations. Several physical features explain the difference between difficult- and easy-to-score targets. Strong correlations exist between the score and DockQ for targets with highly intertwined monomers and many interface contacts. We also develop a new score based on only two physical features that matches the performance of current PPI scoring functions. In addition, we address the more general problem of flexible-body docking by generating and docking intermediate monomer conformations between their bound and unbound forms. We score the docked models and find that the Spearman correlations between the PPI scores and DockQ decrease strongly as the monomers are deformed from their bound conformations. These results emphasize that PPI docking predictions can be improved by focusing on correlations between the PPI score and DockQ and incorporating more discriminating physical features into PPI scoring functions.

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PubMed
Published
2026-01-07
Primary Topic
Protein Structure and Dynamics
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article

Assessment of scoring functions for computational models of protein-protein interfaces.

Jacob Sumner, Corey S. O’Hern
PubMed
Protein Structure and Dynamics
article

Assessment of scoring functions for computational models of protein-protein interfaces.

Jacob Sumner, Corey S. O’Hern
article en

Abstract

An important goal of computational studies of protein-protein interfaces (PPIs) is to predict the binding site between two monomers that form a heterodimer. The simplest version of this problem is to rigidly re-dock the bound forms of the monomers, which involves generating computational models of the heterodimer and then scoring them to determine the most native-like models. PPI scoring functions have been assessed previously using rank- and classification-based metrics; however, these methods are sensitive to the number and quality of models in the scoring function training set. We assess the accuracy of seven PPI scoring functions by comparing their scores of computational models of PPIs to a measure of structural similarity to the x-ray crystal structure (i.e. the DockQ score) for a non-redundant set of heterodimers from the Protein Data Bank. For each heterodimer, we generate re-docked models uniformly sampled over DockQ and calculate the Spearman correlation between the PPI scores and DockQ. For some targets, the scores and DockQ are highly correlated; however, for many targets, there are weak correlations. Several physical features explain the difference between difficult- and easy-to-score targets. Strong correlations exist between the score and DockQ for targets with highly intertwined monomers and many interface contacts. We also develop a new score based on only two physical features that matches the performance of current PPI scoring functions. In addition, we address the more general problem of flexible-body docking by generating and docking intermediate monomer conformations between their bound and unbound forms. We score the docked models and find that the Spearman correlations between the PPI scores and DockQ decrease strongly as the monomers are deformed from their bound conformations. These results emphasize that PPI docking predictions can be improved by focusing on correlations between the PPI score and DockQ and incorporating more discriminating physical features into PPI scoring functions.

PubMed
City College of New York (US), Yale University (US)
Reduced inequalities
Openalex Percentile: Top 85%
Protein Structure and Dynamics
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