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Oligosaccharide recognition and binding to the carbohydrate binding module of AMP‐activated protein kinase
Author(s) -
Koay Ann,
Rimmer Kieran A.,
Mertens Haydyn D.T.,
Gooley Paul R.,
Stapleton David
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.044
Subject(s) - oligosaccharide , biochemistry , carbohydrate , glycogen , ampk , chemistry , protein kinase a , binding site , glycosidic bond , yeast , nuclear magnetic resonance spectroscopy , binding protein , amp activated protein kinase , glycogen synthase , carbohydrate binding module , kinase , enzyme , glycoside hydrolase , stereochemistry , gene
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 15 N 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.