| Literature DB >> 33557270 |
Noriyoshi Manabe1, Yoshiki Yamaguchi1.
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.Entities:
Keywords: 3D structure; Dectin-1; NMR; X-ray crystallography; endoglucanase; triple helix; β-glucan; βGRP/GNBP3
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Year: 2021 PMID: 33557270 PMCID: PMC7915573 DOI: 10.3390/ijms22041578
Source DB: PubMed Journal: Int J Mol Sci ISSN: 1422-0067 Impact factor: 5.923