3D Structural Insights into β-Glucans and Their Binding Proteins

beta(1,3)-glucans are a component of fungal and plant cell walls. The beta-glucan of pathogens is recognized as a non-self-component in the host defense system. Long beta-glucan chains are capable of forming a triple helix structure, and the tertiary structure may profoundly affect the interaction with beta-glucan-binding proteins. Although the atomic details of beta-glucan binding and signaling of cognate receptors remain mostly unclear, X-ray crystallography and NMR analyses have revealed some aspects of beta-glucan structure and interaction. Here, we will review three-dimensional (3D) structural characteristics of beta-glucans and the modes of interaction with beta-glucan-binding proteins.

Automated summary

Beta-glucans are components of fungal and plant cell walls, and are recognized as non-self-components in the host defense system. Their long chains can form a triple helix structure, potentially affecting interactions with beta-glucan-binding proteins. While details of beta-glucan binding and receptor signaling remain unclear, X-ray crystallography and NMR analyses have provided insights into their structure and interactions.