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

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-glu...

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Detalles Bibliográficos
Autores principales: Manabe, Noriyoshi, Yamaguchi, Yoshiki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915573/
https://www.ncbi.nlm.nih.gov/pubmed/33557270
http://dx.doi.org/10.3390/ijms22041578
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author Manabe, Noriyoshi
Yamaguchi, Yoshiki
author_facet Manabe, Noriyoshi
Yamaguchi, Yoshiki
author_sort Manabe, Noriyoshi
collection PubMed
description 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.
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spelling pubmed-79155732021-03-01 3D Structural Insights into β-Glucans and Their Binding Proteins Manabe, Noriyoshi Yamaguchi, Yoshiki Int J Mol Sci Review 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. MDPI 2021-02-04 /pmc/articles/PMC7915573/ /pubmed/33557270 http://dx.doi.org/10.3390/ijms22041578 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Manabe, Noriyoshi
Yamaguchi, Yoshiki
3D Structural Insights into β-Glucans and Their Binding Proteins
title 3D Structural Insights into β-Glucans and Their Binding Proteins
title_full 3D Structural Insights into β-Glucans and Their Binding Proteins
title_fullStr 3D Structural Insights into β-Glucans and Their Binding Proteins
title_full_unstemmed 3D Structural Insights into β-Glucans and Their Binding Proteins
title_short 3D Structural Insights into β-Glucans and Their Binding Proteins
title_sort 3d structural insights into β-glucans and their binding proteins
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7915573/
https://www.ncbi.nlm.nih.gov/pubmed/33557270
http://dx.doi.org/10.3390/ijms22041578
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