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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Main Authors:	Noriyoshi Manabe, Yoshiki Yamaguchi
Format:	Article
Language:	English
Published:	MDPI AG 2021-02-01
Series:	International Journal of Molecular Sciences
Subjects:	β-glucan 3D structure triple helix X-ray crystallography NMR βGRP/GNBP3
Online Access:	https://www.mdpi.com/1422-0067/22/4/1578

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record_format	Article
spelling	doaj-5e20abda159547f4b1ab73c6d05461d02021-02-05T00:04:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-02-01221578157810.3390/ijms220415783D Structural Insights into β-Glucans and Their Binding ProteinsNoriyoshi Manabe0Yoshiki Yamaguchi1Division of Pharmaceutical Physical Chemistry, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, JapanDivision of Pharmaceutical Physical Chemistry, Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japanβ(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.https://www.mdpi.com/1422-0067/22/4/1578β-glucan3D structuretriple helixX-ray crystallographyNMRβGRP/GNBP3
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Noriyoshi Manabe Yoshiki Yamaguchi
spellingShingle	Noriyoshi Manabe Yoshiki Yamaguchi 3D Structural Insights into β-Glucans and Their Binding Proteins International Journal of Molecular Sciences β-glucan 3D structure triple helix X-ray crystallography NMR βGRP/GNBP3
author_facet	Noriyoshi Manabe Yoshiki Yamaguchi
author_sort	Noriyoshi Manabe
title	3D Structural Insights into β-Glucans and Their Binding Proteins
title_short	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_sort	3d structural insights into β-glucans and their binding proteins
publisher	MDPI AG
series	International Journal of Molecular Sciences
issn	1661-6596 1422-0067
publishDate	2021-02-01
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.
topic	β-glucan 3D structure triple helix X-ray crystallography NMR βGRP/GNBP3
url	https://www.mdpi.com/1422-0067/22/4/1578
work_keys_str_mv	AT noriyoshimanabe 3dstructuralinsightsintobglucansandtheirbindingproteins AT yoshikiyamaguchi 3dstructuralinsightsintobglucansandtheirbindingproteins
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3D Structural Insights into β-Glucans and Their Binding Proteins

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