Contribution of Coordinated Substitutions to the Constancy of Physicochemical Properties of ATP-Binding Loop in Protein Kinases

Abstract

It is known that the physicochemical properties of a protein that determine the specific folding of its polypeptide chain and functional features remain stable in the course of evolution. Search for such conserved characteristics by analysis of homologous sequences may aid understanding the function, structure, and evolution of proteins. Coordinated substitutions of amino acid residues are one of the plausible mechanisms maintaining these characteristics. The contribution of coordinated amino acid substitutions to the constancy of several integral physicochemical properties of the ATP-binding loop in protein kinases was studied. It was shown that coordinated substitutions contributed to the conservation of several integral characteristics of the loop related to the charge, hydrophobicity, and β-structure.