Structural changes in glycogen phosphorylase induced by phosphorylation
Authors:
- K. R. AcharyaKAK. R. Acharya
- E. J. GoldsmithEGE. J. Goldsmith
- D. I. StuartDSD. I. Stuart
- K. VarvillKVK. Varvill
- R. J. FletterickRFR. J. Fletterick
- N. B. MadsenNMN. B. Madsen
- L. N. JohnsonLJL. N. Johnson
- 1 November 1988
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 336 (6196) , 215-221
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.Keywords
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