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Title
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Structural changes in glycogen phosphorylase induced by phosphorylation.
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Authors
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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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Ref.
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Nature, 1988,
336,
215-221.
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PubMed id
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Abstract
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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.
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