Abstract
β(1,3)-glucans are a component of fungal and plant cell walls. The β-glucan of pathogens is recognized as a non-self-component in the host defense system. Long β-glucan chains are capable of forming a triple helix structure, and the tertiary structure may profoundly affect the interaction with β-glucan-binding proteins. Although the atomic details of β-glucan binding and signaling of cognate receptors remain mostly unclear, X-ray crystallography and NMR analyses have revealed some aspects of β-glucan structure and interaction. Here, we will review three-dimensional (3D) structural characteristics of β-glucans and the modes of interaction with β-glucan-binding proteins.
Highlights
Variation of β-Glucan Primary StructuresCitation: Manabe, N.; Yamaguchi, Y.Mol
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Accumulating evidence suggests that long-chain β-glucan forms a triple helix structure similar to that of collagen
Summary
Accumulating evidence suggests that long-chain β-glucan forms a triple helix structure similar to that of collagen. Each chain is composed of sixofglucose residues per turn, yielding a pitcha pitch of 2.9–3.0 per residue These parameters indicate thatthat the the backbone conformation of of scleroglucan is similar to that of curdran. Solution studies of shizophyllan by light scattering and viscosity measurement suggest a semi-flexible, rod-like structure with the pitch per glucose residue and the persistence length of the triple helix of 3.0 A and. Laminarin from Laminaria digitata, whose molecular mass is around 5000 Da, is present mostly in a monomeric form with triplex structures a minor population (5%) [16,17] According to these studies, it can be seen that a molecular weight of more than several tens of thousands per one β-glucan chain is necessary to form a stable triple helix.
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