The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114712" target="_blank" >RIV/00216224:14740/20:00114712 - isvavai.cz</a>
Výsledek na webu
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202000593" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/chem.202000593</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/chem.202000593" target="_blank" >10.1002/chem.202000593</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
The CH-pi Interaction in Protein-Carbohydrate Binding: Bioinformatics and In Vitro Quantification
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10600 - Biological sciences
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Chemistry - A European Journal
ISSN
0947-6539
e-ISSN
—
Svazek periodika
26
Číslo periodika v rámci svazku
47
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
12
Strana od-do
10769-10780
Kód UT WoS článku
000552350100001
EID výsledku v databázi Scopus
2-s2.0-85088650259