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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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. |
format | Online Article Text |
id | pubmed-7915573 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT manabenoriyoshi 3dstructuralinsightsintobglucansandtheirbindingproteins AT yamaguchiyoshiki 3dstructuralinsightsintobglucansandtheirbindingproteins |