Structural changes in glycogen phosphorylase induced by phosphorylation.

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...

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书目详细资料
Main Authors: Sprang, SR, Acharya, K, Goldsmith, E, Stuart, D, Varvill, K, Fletterick, R, Madsen, N, Johnson, L
格式: Journal article
语言:English
出版: 1988
实物特征
总结: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.