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MuToN Quantifies Binding Affinity Changes upon Protein Mutations by Geometric Deep Learning
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DOI：10.1002/advs.202402918.png)
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Abstract
En 中文
Assessing changes in protein-protein binding affinity due to mutations helps understanding a wide range of crucial biological processes within cells. Despite significant efforts to create accurate computational models, predicting how mutations affect affinity remains challenging due to the complexity of the biological mechanisms involved. In the present work, a geometric deep learning framework called MuToN is introduced for quantifying protein binding affinity change upon residue mutations. The method, designed with geometric attention networks, is mechanism-aware. It captures changes in the protein binding interfaces of mutated complexes and assesses the allosteric effects of amino acids. Experimental results highlight MuToN's superiority compared to existing methods. Additionally, MuToN's flexibility and effectiveness are illustrated by its precise predictions of binding affinity changes between SARS-CoV-2 variants and the ACE2 complex. A novel geometric deep learning framework is used for predicting the PPI binding affinity change upon mutations. This approach is biological mechanism-aware and makes important advances by considering the protein-protein interaction process and allosteric communications. It surpasses SOTA performances and provides a useful tool for understanding the impact of mutations on biological activity. image
Keywords:
binding affinity
geometric deep learning
mutation
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