Molecular architecture of the glycogen- committed PP1/PTG holoenzyme

Marta Stefania Semrau; Gabriele Giachin; Sonia Covaceuszach; Alberto Cassetta; Nicola Demitri; Paola Storici; Graziano Lolli

doi:10.1038/s41467-022-33693-z

Nature Communications (Oct 2022)

Molecular architecture of the glycogen- committed PP1/PTG holoenzyme

Marta Stefania Semrau,
Gabriele Giachin,
Sonia Covaceuszach,
Alberto Cassetta,
Nicola Demitri,
Paola Storici,
Graziano Lolli

Affiliations

Marta Stefania Semrau: Department of Cellular, Computational and Integrative Biology - CIBio, University of Trento
Gabriele Giachin: Department of Chemical Sciences (DiSC), University of Padua
Sonia Covaceuszach: Institute of Crystallography - C.N.R.- Trieste Outstation
Alberto Cassetta: Institute of Crystallography - C.N.R.- Trieste Outstation
Nicola Demitri: XRD2 Beamline, Elettra Sincrotrone Trieste S.C.p.A
Paola Storici: Protein Facility, Elettra Sincrotrone Trieste S.C.p.A
Graziano Lolli: Department of Cellular, Computational and Integrative Biology - CIBio, University of Trento

DOI: https://doi.org/10.1038/s41467-022-33693-z
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 11

Abstract

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Glycogen metabolism is tightly regulated. Here the authors describe the 3D structure of the PP1/PTG protein complex, which plays a prominent role in the activation of glycogen synthesis and in the pathogenesis of Lafora disease, the most severe form of pediatric progressive epilepsy.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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