A CBM20 low-affinity starch-binding domain from glucan, water dikinase.

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Christiansen C, Hachem MA, Glaring MA, Vikso-Nielsen A, Sigurskjold BW, Svensson B, Blennow A

A CBM20 low-affinity starch-binding domain from glucan, water dikinase.

FEBS Lett. 2009 Apr 2;583(7):1159-63. doi: 10.1016/j.febslet.2009.02.045. Epub 2009 Mar 9.

PubMed ID

19275898 [ View in PubMed

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Abstract

The family 20 carbohydrate-binding module (CBM20) of the Arabidopsis starch phosphorylator glucan, water dikinase 3 (GWD3) was heterologously produced and its properties were compared to the CBM20 from a fungal glucoamylase (GA). The GWD3 CBM20 has 50-fold lower affinity for cyclodextrins than that from GA. Homology modelling identified possible structural elements responsible for this weak binding of the intracellular CBM20. Differential binding of fluorescein-labelled GWD3 and GA modules to starch granules in vitro was demonstrated by confocal laser scanning microscopy and yellow fluorescent protein-tagged GWD3 CBM20 expressed in tobacco confirmed binding to starch granules in planta.

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Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Alglucosidase alfa	Glycogen	Group	Humans	Yes	Cleavage	Details