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@proceedings{1404394, author = {Žufanová, Zuzana and Houser, Josef and Kozmon, Stanislav and Mishra, Deepti and Koča, Jaroslav and Wimmerová, Michaela}, booktitle = {XVIII. setkání biochemiků a molekulárních biologů}, keywords = {CH-pi stacking; carbohydrate-protein interactions; aromatic amino-acid residues; PDB database}, language = {eng}, isbn = {978-80-210-8765-1}, title = {CH-pi stacking interaction in carbohydrate-protein complexes}, year = {2017} }
TY - CONF ID - 1404394 AU - Žufanová, Zuzana - Houser, Josef - Kozmon, Stanislav - Mishra, Deepti - Koča, Jaroslav - Wimmerová, Michaela PY - 2017 TI - CH-pi stacking interaction in carbohydrate-protein complexes SN - 9788021087651 KW - CH-pi stacking KW - carbohydrate-protein interactions KW - aromatic amino-acid residues KW - PDB database N2 - Interactions of saccharides with receptors belong to the most important ones as in cell recognition, growth or differentiation and in many diseases. These interactions are mediated by so-called glycocode – saccharide code which is read by many proteins. There are several ways how saccharides interact with proteins: hydrogen bridges, metal-ion-mediated interaction etc. The role of dispersion-driven CH-pi interactions in protein-carbohydrate interactions has been underestimated for a long time. This type of interaction occurs between carbohydrate apolar faces and aromatic amino-acid residues. The CH-pi stacking is a non-covalent interaction where a CH group interacts with an aromatic ring and can be recognized as a special type of the hydrogen bond. We investigated CH-pi stacking interactions in protein/carbohydrate complexes by the bioinformatic structure-based study. The Protein Data Bank (PDB) database has been used as a source of structural data of the carbohydrate/protein complexes. The database contains more than 10 000 entries of protein complexes with carbohydrates. We have searched the PDB database to examine complexes with carbohydrates in a close proximity of the aromatic amino acid (tryptophan, tyrosine, phenylalanine, and histidine). In these complexes, we have found that CH-pi stacking is highly important interaction, being detected in 61 % of these complexes. The analysis has shown that the most frequent residue involved in the CH-pi stacking complexes is tryptophan. We have also identified the differences in the interaction preferences between individual aromatic amino acid residues and carbohydrates. Our findings may help in a better description of carbohydrate-protein interaction and thus help in drug development, receptor studies or protein engineering. ER -
ŽUFANOVÁ, Zuzana, Josef HOUSER, Stanislav KOZMON, Deepti MISHRA, Jaroslav KOČA and Michaela WIMMEROVÁ. CH-pi stacking interaction in carbohydrate-protein complexes. In \textit{XVIII. setkání biochemiků a molekulárních biologů}. 2017. ISBN~978-80-210-8765-1.
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