The analysis of CH–π interaction in protein–carbohydrate binding

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00129957" target="_blank" >RIV/00216224:14740/21:00129957 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S0108767321090073" target="_blank" >http://dx.doi.org/10.1107/S0108767321090073</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S0108767321090073" target="_blank" >10.1107/S0108767321090073</a>

Jazyk výsledku

angličtina

Název v původním jazyce

The analysis of CH–π interaction in protein–carbohydrate binding

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-π 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. Using the Protein Data Bank (PDB) structural data, we analyzed the CH-π interactions employing bioinformatics (data mining, structural analysis), several experimental (ITC, X-ray crystallography) and computational techniques. Within 12 000 protein complexes with carbohydrates from PDB, the stacking interactions were found in about 39% of them. The calculations and the ITC measurement results suggest that the CH-π stacking contribution to the overall binding energy ranges from 4 kcal/mol up to 8 kcal/mol. All the results show that the stacking CH-π interactions in protein-carbohydrate complexes can be considered to be a driving force of the binding in such complexes.

Název v anglickém jazyce

The analysis of CH–π interaction in protein–carbohydrate binding

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-π 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. Using the Protein Data Bank (PDB) structural data, we analyzed the CH-π interactions employing bioinformatics (data mining, structural analysis), several experimental (ITC, X-ray crystallography) and computational techniques. Within 12 000 protein complexes with carbohydrates from PDB, the stacking interactions were found in about 39% of them. The calculations and the ITC measurement results suggest that the CH-π stacking contribution to the overall binding energy ranges from 4 kcal/mol up to 8 kcal/mol. All the results show that the stacking CH-π interactions in protein-carbohydrate complexes can be considered to be a driving force of the binding in such complexes.

Druh

O - Ostatní výsledky

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

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)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů