Dynamic characteristics of totally glycosylated human glucocerebrosidase carrying N370S substitution

Abstract

Abstract Full-atom models of a totally glycosylated wild type human glucocerebrosidase (GBA) and its mutant form N370S were constructed. Molecular dynamics simulations in explicit water box have revealed high flexibility and mobility of glycans bonded to the enzyme; glycans was able to spread a rather large volume determined by their length. Amino acid substitution N370S decreased the flexibility of GBA polypeptide chain region forming Loop 1 (residues 311-319), while the mobility of catalytic residues remained at the similar level both in wild type and N370S GBA mutant form.