Journal article
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase
Jesse I Mobbs, Ann Koay, Alex Di Paolo, Michael Bieri, Emma J Petrie, Michael A Gorman, Larissa Doughty, Michael W Parker, David I Stapleton, Michael DW Griffin, Paul R Gooley
Biochemical Journal | PORTLAND PRESS LTD | Published : 2015
DOI: 10.1042/BJ20150270
Abstract
AMP-activated protein kinase (AMPK) is an αβγ heterotrimer that is important in regulating energy metabolism in all eukaryotes. The β-subunit exists in two isoforms (β1 and β2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (β1- and β2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. β2-CBM binds linear carbohydrates with 4-fold greater affinity than β1-CBM and binds single α1,6-branched carbohydrates up to 30-fold tighter. To understand these affinity differences, especially for branched carbohydrates, we determined the NMR solution structure of β2-CBM in complex with the single α1,..
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Awarded by Australian Research Council
Awarded by National Health and Medical Research Council of Australia
Funding Acknowledgements
This work was supported by the Australian Research Council [grant number DP110103161 (to P.R.G., D.S. and M.W.P.)]; the State of Victoria; the Rowden White Foundation; the Victorian Government Operational Infrastructure Support Scheme; the C.R. Roper Fellowship (to M.D.W.G.); the Australian Research Council Future Fellowship [grant number FT140100544]; and the National Health and Medical Research Council of Australia [grant number 1021645 (to M.W.P.)].