title: Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-beta-glucosidase mutant that causes Gaucher disease.
abstract: Recently, two studies were published that examined the structure of the acid-β-glucosidase N370S mutant, the most common mutant that causes Gaucher disease. One study used the experimental tool of X-ray crystallography, and the other utilized molecular dynamics (MD). The two studies reinforced each other through the similarities in their findings, but each approach also added some unique information. Both studies report that the conformation of active site loop 3 changes, due to an altered hydrogen bonding network; however, the MD study produced additional data concerning the flexibility of loop 1 and the catalytic residues that are not observed in the other study.
authors: Institut für Informatik/I12, Technische Universität München, Boltzmannstr 3, 85748 Garching b. München, Germany. offman@rostlab.org
authors: Marc N
authors: MN
authors: Offman
authors: Marcin
authors: M
authors: Krol
authors: Burkhard
authors: B
authors: Rost
authors: Israel
authors: I
authors: Silman
authors: Joel L
authors: JL
authors: Sussman
authors: Anthony H
authors: AH
authors: Futerman
mesh_terms: D000818:Animals; D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods*; D005776:Gaucher Disease / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D005962:Glucosylceramidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006860:Hydrogen Bonding; D056004:Molecular Dynamics Simulation; D009154:Mutation
chemical_list: D005962:Glucosylceramidase