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

Research output: Contribution to journalArticlepeer-review

281 Scopus citations

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
Pages (from-to)215-221
Number of pages7
JournalNature
Volume336
Issue number6196
DOIs
StatePublished - 1988

Funding

Funder number
R01DK031507

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