Crystal structure of an enzyme involved in Gaucher disease

Greg Petsko and Dagmar Ringe groups (Brandeis University)

 

Gregory Petsko's and Dagmar Ringe's group at Brandeis University have solved several structures using data from the GM/CA sector, including the molecular replacement solution of human acid-beta-glucosidase (GCase) in complex with a pharmacological chaperone. Mutations in this lysosomal enzyme result in Gaucher disease, the most common lysosomal disorder. The pharmacological compound, isofagomine (IFG), induces the active form of the enzyme and improves trafficking of the mutant enzyme to the lysosome.

Figure: Structure of GCase complexed with the drug IFG in the active site.

 

Citation:
Lieberman, RL, Wustman, BA, Huertas, P, Powe Jr, AC, Pine, CW, Khanna, R, Schlossmacher, MG, Ringe, D, Petsko, GA. Structure of acid [beta]-glucosidase with pharmacological chaperone provides insight into Gaucher disease, Nat. Chem. Biol. 3 (2), 101-107 (2007). DOI: 10.1038/nchembio850.

 

 


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