Publications by authors named "Alex Di Paolo"
The β subunit of adenosine monophosphate (AMP)-activated protein kinase (AMPK), which exists as two isoforms (β1 and β2) in humans, has a carbohydrate-binding module (CBM) that interacts with glycogen. Although the β1- and β2-CBMs are structurally similar, with strictly conserved ligand-contact residues, they show different carbohydrate affinities. β2-CBM shows the strongest affinity for both branched and unbranched oligosaccharides and it has recently been shown that a Thr insertion into β2-CBM (Thr101) forms a pocket to accommodate branches.
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- AMP-activated protein kinase (AMPK) plays a crucial role in regulating energy metabolism across all eukaryotes and has different isoforms of its β-subunit that affect its carbohydrate-binding capabilities.
- The β2-CBM isoform displays significantly higher affinity for linear carbohydrates and even greater affinity for branched carbohydrates compared to the β1-CBM isoform, as determined through structural analysis.
- Structural studies, including NMR and X-ray crystallography, reveal how the β2-CBM's unique amino acid structure allows it to form specific interactions with α1,6 branches, indicating that AMPK with the β2 isoform may more effectively bind to partially degraded glycogen.