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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 publication

DOI

10.1038/336215a0

Type

Journal article

Journal

Nature

Publication Date

17/11/1988

Volume

336

Pages

215 - 221

Keywords

Adenosine Monophosphate, Allosteric Site, Chemical Phenomena, Chemistry, Physical, Enzyme Activation, Glucose-6-Phosphate, Glucosephosphates, Hydrogen Bonding, Macromolecular Substances, Phosphorylases, Phosphorylation, Phosphoserine, Protein Conformation, X-Ray Diffraction