Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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