Publication details

The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification

Authors

HOUSER Josef KOZMON Stanislav MISHRA Deepti HAMMEROVÁ Zuzana WIMMEROVÁ Michaela KOČA Jaroslav

Year of publication 2020
Type Article in Periodical
Magazine / Source Chemistry - A European Journal
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202000593
Doi http://dx.doi.org/10.1002/chem.202000593
Keywords carbohydrates; density functional calculations; glycosylation; ligand binding; stacking interaction
Description The molecular recognition of carbohydrates by proteins plays a key role in many biological processes including immune response, pathogen entry into a cell, and cell-cell adhesion (e.g., in cancer metastasis). Carbohydrates interact with proteins mainly through hydrogen bonding, metal-ion-mediated interaction, and non-polar dispersion interactions. The role of dispersion-driven CH-pi interactions (stacking) in protein-carbohydrate recognition has been underestimated for a long time considering the polar interactions to be the main forces for saccharide interactions. However, over the last few years it turns out that non-polar interactions are equally important. In this study, we analyzed the CH-pi interactions employing bioinformatics (data mining, structural analysis), several experimental (isothermal titration calorimetry (ITC), X-ray crystallography), and computational techniques. The Protein Data Bank (PDB) has been used as a source of structural data. The PDB contains over 12 000 protein complexes with carbohydrates. Stacking interactions are very frequently present in such complexes (about 39 % of identified structures). The calculations and the ITC measurement results suggest that the CH-pi stacking contribution to the overall binding energy ranges from 4 up to 8 kcal mol(-1). All the results show that the stacking CH-pi interactions in protein-carbohydrate complexes can be considered to be a driving force of the binding in such complexes.
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