Journal article

Structural basis for glycogen recognition by AMP-activated protein kinase

G Polekhina, A Gupta, BJW van Denderen, SC Fell, BE Kemp, D Stapleton, MW Parker

Structure | CELL PRESS | Published : 2005

Abstract

AMP-activated protein kinase (AMPK) coordinates cellular metabolism in response to energy demand as well as to a variety of stimuli. The AMPK beta subunit acts as a scaffold for the alpha catalytic and gamma regulatory subunits and targets the AMPK heterotrimer to glycogen. We have determined the structure of the AMPK beta glycogen binding domain in complex with beta-cyclodextrin. The structure reveals a carbohydrate binding pocket that consolidates all known aspects of carbohydrate binding observed in starch binding domains into one site, with extensive contact between several residues and five glucose units. beta-cyclodextrin is held in a pincer-like grasp with two tryptophan residues crad..

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