An NMR analysis of the binding of inhibitors to yeast phosphoglycerate kinase.
The binding of a series of inhibitors to the enzyme phosphoglycerate kinase has been studied using NMR to uncover the binding sites and the effects of binding on the protein conformation. The very effective inhibitor, Suramin, causes the most pronounced changes. The design of inhibitors for mobile proteins is discussed.
Boyle
H A
HA
Inorganic Chemistry Laboratory, University of Oxford, England.
Fairbrother
W J
WJ
Williams
R J
RJ
D001665:Binding Sites; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D063065:Organophosphonates / Q000378:metabolism; D010735:Phosphoglycerate Kinase / Q000037:antagonists & inhibitors*; D011487:Protein Conformation; D013498:Suramin / Q000378:metabolism; D015003:Yeasts / Q000201:enzymology*
D063065:Organophosphonates; D013498:Suramin; D010735:Phosphoglycerate Kinase