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.
Original language | English |
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Pages (from-to) | 215-221 |
Number of pages | 7 |
Journal | Nature |
Volume | 336 |
Issue number | 6196 |
DOIs | |
State | Published - 1988 |