Structure of Galectin-3 bound to a model membrane containing ganglioside GM1.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
06 06 2023
06 06 2023
Historique:
received:
06
07
2022
revised:
05
08
2022
accepted:
15
08
2022
pmc-release:
06
06
2024
medline:
9
6
2023
pubmed:
21
8
2022
entrez:
20
8
2022
Statut:
ppublish
Résumé
Galectin-3 (Gal-3) is a β-galactosidase-binding protein involved in various biological processes, including neuronal growth and adhesion. The pairing of Gal-3 with ganglioside GM1's pentasaccharide chain at the outer leaflet of the plasma membrane, which triggers downstream cell-signaling cascades, seems to be involved in these processes. A crucial feature of Gal-3 is its ability to form oligomers and supramolecular assemblies that connect various carbohydrate-decorated molecules. Although we know the atomistic structure of Gal-3 bound to small carbohydrate ligands, it remains unclear how Gal-3 binds GM1 in a membrane. Furthermore, the influence of this interaction on Gal-3's structure and oligomeric assembly has to be elucidated. In this study, we used X-ray reflectivity (XR) from a model membrane to determine the structure and surface coverage of Gal-3 bound to a membrane containing GM1. We observed that the carbohydrate recognition domain interacts with GM1's pentasaccharide, while the N-terminal domain is pointed away from the membrane, likely to facilitate protein-protein interactions. In a membrane containing 20 mol % GM1, Gal-3 covered ∼50% of the membrane surface with one Gal-3 molecule bound per 2130 Å
Identifiants
pubmed: 35986516
pii: S0006-3495(22)00678-6
doi: 10.1016/j.bpj.2022.08.018
pmc: PMC10257012
pii:
doi:
Substances chimiques
G(M1) Ganglioside
37758-47-7
Galectin 3
0
Gangliosides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1926-1937Subventions
Organisme : NINDS NIH HHS
ID : R25 NS080685
Pays : United States
Informations de copyright
Copyright © 2022 Biophysical Society. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no conflict of interest.
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