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Structure of human lysosomal enzyme GALNS

Research Achievements

Structure of human lysosomal enzyme GALNS

Yadilette Rivera-Colón (ICE IGERT associate, molecular and cellular biology) published an article entitled: “The Structure of Human GALNS Reveals the Molecular Basis for Mucopolysaccharidosis IV A” in the Journal of Molecular Biology. Yadilette studies lysosomal storage diseases, which are disorders caused by deficiencies of enzymes responsible for the degradation of substances present in lysosomes. The human lysosomal enzyme galactosamine-6-sulfatase (GALNS) is deficient in patients with the lysosomal storage disease mucopolysaccharidosis IV A. Yadilette and the team determined the three-dimensional structure of human GALNS by X-ray crystallography. The structure reveals that the active site of GALNS is a large, positively charged trench suitable for binding negatively charged substrates such as keratan sulfate and chondroitin-6-sulfate. Yadilette’s beautiful visual representation of this concept was selected for the cover image (volume 424, issues 1-2).