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


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,..

View full abstract


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.)].