1FA9

HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP

Summary for 1FA9

• Entry DOI: 10.2210/pdb1fa9/pdb
• Related: 1FC0
• Descriptor: GLYCOGEN PHOSPHORYLASE, LIVER FORM, alpha-D-glucopyranose, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• Functional Keywords: protein-ligand complex, allosteric protein, phosphorylated protein, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 97999.77

Authors

Rath, V.L.,Ammirati, M.,LeMotte, P.K.,Fennell, K.F.,Mansour, M.N.,Danley, D.E.,Hynes, T.R.,Schulte, G.K.,Wasilko, D.J.,Pandit, J. (deposition date: 2000-07-12, release date: 2000-08-25, Last modification date: 2023-08-09)

Primary citation

Rath, V.L.,Ammirati, M.,LeMotte, P.K.,Fennell, K.F.,Mansour, M.N.,Danley, D.E.,Hynes, T.R.,Schulte, G.K.,Wasilko, D.J.,Pandit, J.
Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core.
Mol.Cell, 6:139-148, 2000

PubMed Abstract: Glycogen phosphorylases catalyze the breakdown of glycogen to glucose-1-phosphate, which enters glycolysis to fulfill the energetic requirements of the organism. Maintaining control of blood glucose levels is critical in minimizing the debilitating effects of diabetes, making liver glycogen phosphorylase a potential therapeutic target. To support inhibitor design, we determined the crystal structures of the active and inactive forms of human liver glycogen phosphorylase a. During activation, forty residues of the catalytic site undergo order/disorder transitions, changes in secondary structure, or packing to reorganize the catalytic site for substrate binding and catalysis. Knowing the inactive and active conformations of the liver enzyme and how each differs from its counterpart in muscle phosphorylase provides the basis for designing inhibitors that bind preferentially to the inactive conformation of the liver isozyme.

PubMed: 10949035
DOI: 10.1016/S1097-2765(00)00015-0

Experimental method

X-RAY DIFFRACTION (2.4 Å)