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- W4385236095 abstract "Abstract Dynamics-driven allostery provides important insights into the working mechanics of proteins, especially enzymes. In this study we employ this paradigm to answer a basic question: in enzyme superfamilies where the catalytic mechanism, active sites and protein fold are conserved, what accounts for the difference in the catalytic prowess of the individual members? We show that when subtle changes in sequence do not translate to changes in structure, they do translate to changes in dynamics. We use sequentially diverse PTP1B, TbPTP1, and YopH as the representatives of the conserved Protein Tyrosine Phosphatase (PTP) superfamily. Using amino acid network analysis of group behavior (community analysis) and influential node dominance on networks (eigenvector centrality), we explain the dynamic basis of catalytic variations seen between the three proteins. Importantly, we explain how a dynamics-based blueprint makes PTP1B amenable to allosteric control and how the same is abstracted in TbPTP1 and YopH." @default.
- W4385236095 created "2023-07-26" @default.
- W4385236095 creator A5028245832 @default.
- W4385236095 creator A5030956462 @default.
- W4385236095 date "2023-07-25" @default.
- W4385236095 modified "2023-10-16" @default.
- W4385236095 title "Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics" @default.
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