Small-angle X-ray scattering to obtain ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
Small-angle X-ray scattering to obtain models of multivalent lectin-glycan complexes
Auteur(s) :
Weeks, Stephen D. [Auteur]
Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
Bouckaert, Julie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Titre de la revue :
Methods in molecular biology (Clifton, N.J.)
Nom court de la revue :
Methods Mol. Biol.
Numéro :
1200
Pagination :
511-526
Date de publication :
2014-07-22
ISSN :
1940-6029
Mot(s)-clé(s) en anglais :
Protein Structure, Tertiary
Animals
Protein Structure, Secondary
Cattle
X-Ray Diffraction
Models, Molecular
Scattering, Small Angle
Lectins
Polysaccharide
Bacterial Proteins
Animals
Protein Structure, Secondary
Cattle
X-Ray Diffraction
Models, Molecular
Scattering, Small Angle
Lectins
Polysaccharide
Bacterial Proteins
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Recent advances in small-angle X-ray scattering (SAXS) have led to the ability to model the glycans on glycoproteins and to obtain the low-resolution solution structures of complexes of lectins bound to multivalent ...
Lire la suite >Recent advances in small-angle X-ray scattering (SAXS) have led to the ability to model the glycans on glycoproteins and to obtain the low-resolution solution structures of complexes of lectins bound to multivalent glycan-presenting scaffolds. This progress in SAXS can respond to the increasing interest in the biological action of glycoproteins and lectins and in the design of multivalent glycan-based antagonists. Carbohydrates make up a significant part of the X-ray scattering content in SAXS and should be included in the model together with the protein, whose structure is most often based on a crystal structure or NMR ensemble, to give a far-improved fit with the experimental data. The modeling of the spatial positioning of glycans on proteins or in the architecture of lectin-glycan complexes delivers low-resolution structural information hitherto unmatched by any other method. SAXS data on the bacterial lectin FimH, strongly bound to heptyl α-D-mannose on a sevenfold derivatized β-cyclodextrin, permitted determination of the stoichiometry of the complex and the geometry of the lectin deposition on the multivalent β-cyclodextrin. The SAXS methods can be applied to larger complexes as the technique imposes no limit on the size of the macromolecular assembly in solution.Lire moins >
Lire la suite >Recent advances in small-angle X-ray scattering (SAXS) have led to the ability to model the glycans on glycoproteins and to obtain the low-resolution solution structures of complexes of lectins bound to multivalent glycan-presenting scaffolds. This progress in SAXS can respond to the increasing interest in the biological action of glycoproteins and lectins and in the design of multivalent glycan-based antagonists. Carbohydrates make up a significant part of the X-ray scattering content in SAXS and should be included in the model together with the protein, whose structure is most often based on a crystal structure or NMR ensemble, to give a far-improved fit with the experimental data. The modeling of the spatial positioning of glycans on proteins or in the architecture of lectin-glycan complexes delivers low-resolution structural information hitherto unmatched by any other method. SAXS data on the bacterial lectin FimH, strongly bound to heptyl α-D-mannose on a sevenfold derivatized β-cyclodextrin, permitted determination of the stoichiometry of the complex and the geometry of the lectin deposition on the multivalent β-cyclodextrin. The SAXS methods can be applied to larger complexes as the technique imposes no limit on the size of the macromolecular assembly in solution.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Computational Molecular Systems Biology
Date de dépôt :
2020-02-12T15:11:24Z
2021-04-21T07:55:15Z
2021-04-21T07:55:15Z