Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis.

doi:10.1016/j.jmb.2006.04.004

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Article

Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis.

Journal of molecular biology - 16 Jun 2006

Lemieux M Joanne, Mark Brian L, Cherney Maia M, Withers Stephen G, Mahuran Don J, James Michael N G

Abstract excerpt

Lysosomal beta-hexosaminidase A (Hex A) is essential for the degradation of GM2 gangliosides in the central and peripheral nervous system. Accumulation of GM2 leads to severely debilitating neurodegeneration associated with Tay-Sachs disease (TSD), Sandoff disease (SD) and AB variant. Here, we present the X-ray crystallographic structure of Hex A to 2.8 A resolution and the structure of Hex A in complex with...

Topics

Acetylglucosamine
Amino Acid Substitution
Arginine
Aspartic Acid
Binding Sites
Crystallography, X-Ray
Dimerization
Gangliosidoses, GM2
Glycine
Glycosylation
Hexosaminidase A
Humans
Hydrolysis

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Mutation

Protein Conformation

Protein Subunits

Tay-Sachs Disease

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Identifiers

PMID: 16698036
DOI: 10.1016/j.jmb.2006.04.004
PMCID: PMC2910082

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