The AMP-activated protein kinase (AMPK) contains a carbohydrate-binding module (β1-CBM) that is conserved from yeast to mammals. β1-CBM has been shown to localize AMPK to glycogen in intact cells and in vitro. Here we use Nuclear Magnetic Resonance spectroscopy to investigate oligosaccharide binding to 15N labelled β1-CBM. We find that β1-CBM shows greatest affinity to carbohydrates of greater than five glucose units joined via α,1 → 4 glycosidic linkages with a single, but not multiple, glucose units in an α,1 → 6 branch. The near identical chemical shift profile for all oligosaccharides whether cyclic or linear suggest a similar binding conformation and confirms the presence of a single carbohydrate-binding site. © 2007 Federation of European Biochemical Societies.
Koay, A., Rimmer, K. A., Mertens, H. D. T., Gooley, P. R., & Stapleton, D. (2007). Oligosaccharide recognition and binding to the carbohydrate binding module of AMP-activated protein kinase. FEBS Letters, 581(26), 5055–5059. https://doi.org/10.1016/j.febslet.2007.09.044