Abstract
To summarise the first part of this thesis, I have demonstrated the utility of protein X-ray crystal structures containing carbohydrates as a source of information on PCIs. I generated a database of coordinates of carbohydrate residues and proximal amino acids from structures in the PDB (Berman et al., Nucl Acids Res 28:235–242, 2000, [1]), with the carbohydrates identified using GlyVicinity, (Lütteke and Frank, Nucl Acids Res 33:D242–D246, 2005, [2]) and the quality of the data validated using Privateer (Agirre et al., Nat Struct Mol Biol 22:833–834, 2015, [3]). Analysis of the distribution of amino acids in the carbohydrate binding sites, and particularly comparison of the distributions around different monosaccharides, are powerful tools for understanding carbohydrate-based interactions at the molecular level.
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Hudson, K.L. (2018). Conclusions and Future Directions. In: Carbohydrate-Based Interactions at the Molecular and the Cellular Level. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-77706-1_6
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DOI: https://doi.org/10.1007/978-3-319-77706-1_6
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