Allosteric interactions of glycogen phosphorylase b. A crystallographic study of glucose 6-phosphate and inorganic phosphate binding to di-imidate-cross-linked phosphorylase b.

The binding to glycogen phosphorylase b of glucose 6-phosphate and inorganic phosphate (respectively allosteric inhibitor and substrate/activator of the enzyme) were studied in the crystal at 0.3 nm (3A) resolution. Glucose 6-phosphate binds in the alpha-configuration at a site that is close to the...

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Bibliographic Details
Main Authors: Lorek, A, Wilson, K, Sansom, MS, Stuart, D, Stura, E, Jenkins, J, Zanotti, G, Hajdu, J, Johnson, L
Format: Journal article
Language:English
Published: 1984