| Autor: |
Sprang, S. R., Acharya, K. R., Goldsmith, E. J., Stuart, D. I., Varvill, K., Fletterick, R. J., Madsen, N. B., Johnson, L. N. |
| Zdroj: |
Nature; November 1988, Vol. 336 Issue: 6196 p215-221, 7p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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