Publication: Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation
Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation
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Riemersma, M., Froese, D. S., van Tol, W., & et al. (2015). Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation. Chemistry & Biology, 22(12), 1643–1652. https://doi.org/10.1016/j.chembiol.2015.10.014
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A unique, unsolved O-mannosyl glycan on α-dystroglycan is essential for its interaction with protein ligands in the extracellular matrix. Defective O-mannosylation leads to a group of muscular dystrophies, called dystroglycanopathies. Mutations in isoprenoid synthase domain containing (ISPD) represent the second most common cause of these disorders, however, its molecular function remains uncharacterized. The human ISPD (hISPD) crystal structure showed a canonical N-terminal cytidyltransferase domain linked to a C-terminal domain that
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- Riemersma, Moniek
- van Tol, Walinka
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Riemersma, M., Froese, D. S., van Tol, W., & et al. (2015). Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation. Chemistry & Biology, 22(12), 1643–1652. https://doi.org/10.1016/j.chembiol.2015.10.014
