Structural changes in glycogen phosphorylase induced by phosphorylation

S. R. Sprang, K. R. Acharya, E. J. Goldsmith, D. I. Stuart, K. Varvill, R. J. Fletterick, N. B. Madsen, L. N. Johnson

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Abstract

A comparison of the refined crystal structures of dimeric glycogen phosphorylase b and a reveals structural changes that represent the first step in the activation of the enzyme. On phosphorylation of serine-14, the N-terminus of each subunit assumes an ordered helical conformation and binds to the surface of the dimer. The consequent structural changes at the N- and C-terminal regions lead to strengthened interactions between subunits and alter the binding sites for allosteric effectors and substrates.

Original languageEnglish (US)
Pages (from-to)215-221
Number of pages7
JournalNature
Volume336
Issue number6196
DOIs
StatePublished - Jan 1 1988

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Sprang, S. R., Acharya, K. R., Goldsmith, E. J., Stuart, D. I., Varvill, K., Fletterick, R. J., Madsen, N. B., & Johnson, L. N. (1988). Structural changes in glycogen phosphorylase induced by phosphorylation. Nature, 336(6196), 215-221. https://doi.org/10.1038/336215a0