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

278 Scopus citations


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
Issue number6196
StatePublished - 1988


Dive into the research topics of 'Structural changes in glycogen phosphorylase induced by phosphorylation'. Together they form a unique fingerprint.

Cite this