Structural changes in glycogen phosphorylase induced by phosphorylation |
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| Authors: | S R Sprang K R Acharya E J Goldsmith D I Stuart K Varvill R J Fletterick N B Madsen L N Johnson |
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| Institution: | Department of Biochemistry, University of Texas Southwestern Medical Centre, Dallas 75235-9050. |
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| 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. |
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