Additive energetic contributions of multiple peptide positions determine the relative promiscuity of viral and human sequences for PDZ domain targets

Abstract excerpt

Protein-protein interactions that include recognition of short sequences of amino acids, or peptides, are critical in cellular processes. Protein-peptide interaction surface areas are relatively small and shallow, and there are often overlapping specificities in families of peptide-binding domains. Therefore, dissecting selectivity determinants can be challenging. PDZ domains are an example of a peptide-binding do...

Topics

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• Binding Sites
• Computational Biology
• Intrinsically Disordered Proteins
• Models, Molecular
• Mutation
• PDZ Domains
• Protein Binding
• Thermodynamics

Identifiers and source

Literature Corpus work

d94a58a4-eaad-5e36-afb4-7ee4b18fd950

DOI

10.1101/2022.12.31.522388