CH-π interactions confer orientational flexibility in protein-carbohydrate binding sites.

ABSTRACT: Protein-carbohydrate binding plays an essential role in biological processes including cellular recognition and immune signaling. However, glycans are hydrophilic with limited hydrophobic surfaces, a challenge for selective recognition by proteins. CH-π stacking interactions are pervasive in protein-carbohydrate binding sites and have emerged as critical drivers of protein-carbohydrate recognition. These interactions are highly favorable and have a broad orientational landscape. However, it is unknown how the orientations of CH-π stacking interactions are influenced by the protein environment; their functional interplay with hydrogen bonds in protein-carbohydrate binding is also unclear. Here, we employ well-tempered metadynamics simulations to obtain binding free energy landscapes for a s

SUBMITTER: Keys AM 

PROVIDER: S-EPMC12309604 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature