| Popis: |
Glycogen phosphorylase, the archetypal allosteric enzyme, is also metabolically interconvertible between physiologically active and inactive forms in response to hormonal and nervous controls. The crystal structure of the a (active) form at 3.0 A resolution, together with ligand binding studies, reveals the nature of the sub-unit interactions in relation to the active sites, demonstrates the interrelationships of the various binding sites, and suggests molecular mechanisms for the allosteric and metabolic regulation. |
