Structural changes in glycogen phosphorylase induced by phosphorylation
- 1 November 1988
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 336 (6196), 215-221
- https://doi.org/10.1038/336215a0
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 substratesKeywords
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