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Enzyme Research
Volume 2011, Article ID 973231, 15 pages
Review Article

A Guided Tour of the Structural Biology of Gaucher Disease: Acid-β-Glucosidase and Saposin C

School of Chemistry & Biochemistry, Institute for Bioscience and Bioengineering, Georgia Institute of Technology, 901 Atlantic Drive NW Atlanta, GA 30332-0400, USA

Received 13 May 2011; Accepted 7 September 2011

Academic Editor: Mia Horowitz

Copyright © 2011 Raquel L. Lieberman. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Mutations in both acid-β-glucosidase (GCase) and saposin C lead to Gaucher disease, the most common lysosomal storage disorder. The past several years have seen an explosion of structural and biochemical information for these proteins, which have provided new insight into the biology and pathogenesis of Gaucher disease, as well as opportunities for new therapeutic directions. Nearly 20 crystal structures of GCase are now available, from different heterologous sources, complexed with different ligands in the active site, in different glycosylation states, as well as one that harbors a prevalent disease-causing mutation, N370S. For saposin C, two NMR and 3 crystal structures have been solved, each with its unique snapshot. This review focuses on the details of these structures to highlight salient common and disparate features that contribute to our current state of knowledge of this complex orphan disease.