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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 

In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor.

The N-terminal, extracellular domain of the receptor for glucagon-like peptide 1 ( GLP-1 receptor) was expressed at a high level in E. coli and isolated as inclusion bodies. Renaturation with concomitant disulfide bond formation was achieved from guanidinium-solubilized material. A soluble and active fraction of the protein was isolated by ion exchange chromatography and gel filtration. Complex formation with GLP-1 was shown by cross-linking experiments, surface plasmon resonance measurements, and isothermal titration calorimetry. The existence of disulfide bridges in the N-terminal receptor fragment was proven after digestion of the protein with pepsin. Further analysis revealed a disulfide-binding pattern with links between cysteines 46 and 71, 62 and 104, and between 85 and 126.[1]

References

  1. In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor. Bazarsuren, A., Grauschopf, U., Wozny, M., Reusch, D., Hoffmann, E., Schaefer, W., Panzner, S., Rudolph, R. Biophys. Chem. (2002)
 
 
 
 
 
 
 
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