Quantitative mapping of binding specificity landscapes for homologous targets by using a high-throughput method.

ABSTRACT: To facilitate investigations of protein-protein interactions (PPIs), we developed a novel platform for quantitative mapping of protein binding specificity landscapes, which combines the multi-target screening of a mutagenesis library into high- and low-affinity populations with sophisticated next-generation sequencing analysis. Importantly, this method generates accurate models to predict affinity and specificity values for any mutation within a protein complex, and requires only a few experimental binding affinity measurements using purified proteins for calibration. We demonstrated the utility of the approach by mapping quantitative landscapes for interactions between the N-terminal domain of the tissue inhibitor of metalloproteinase 2 (N-TIMP2) and three matrix metalloproteinases (MMPs)

SUBMITTER: Aharon L 

PROVIDER: S-EPMC7376575 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature