Highlights of our Work
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Nearly 80% of the patients suffering from glycogen storage disease have a single mutation in their genome. The product of this gene mediates critical steps in sugar metabolism and storage. However, the molecular basis for the malfunction caused by this and similar mutations has remained unknown due to a lack of structural data. The advent of AlphaFold provided us with the first model of this important protein. As reported in a recent publication in PNAS Nexus, Resource researchers have produced large conformational ensembles of this protein in the empty and sugar-bound forms for both native and 10 clinically-relevant mutants. By identifying the structural and energetic effects of such mutations, using NAMD and VMD, we have begun to elucidate the role of each residue in the dysfunction of the enzyme.