1fa9: Difference between revisions

Revision as of 02:56, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fa9.png

Template:STRUCTURE 1fa9

HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMPHUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP

Template:ABSTRACT PUBMED 10949035

About this StructureAbout this Structure

1FA9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Activation of human liver glycogen phosphorylase by alteration of the secondary structure and packing of the catalytic core., Rath VL, Ammirati M, LeMotte PK, Fennell KF, Mansour MN, Danley DE, Hynes TR, Schulte GK, Wasilko DJ, Pandit J, Mol Cell. 2000 Jul;6(1):139-48. PMID:10949035

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OCA

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+===HUMAN LIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP===
-==Overview==
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-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.
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 [[Category: Phosphorylated protein]]
 [[Category: Protein-ligand complex]]
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