Abstract
Allostery is an intrinsic property of proteins that regulates function. We explored the role of allostery in disease development, particularly for Glucocerebrosidase (GCase). There are over 200 prevalent missense variants in GCase in human populations leading to Gaucher disease (GD). We analyzed four well-known missense GD mutations that are distal to the active site yet impact enzymatic activity. Our site-specific dynamics-based metric reveals that, in GCase, enzymatic function is regulated by dynamically-coupled residues, which forms an allosteric communication network with the active sites.
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