Academic Journal
Impact of sialic acids on the molecular dynamic of bi-antennary and tri-antennary glycans
| العنوان: | Impact of sialic acids on the molecular dynamic of bi-antennary and tri-antennary glycans |
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| المؤلفون: | Guillot, Alexandre, Dauchez, Manuel, Belloy, Nicolas, Jonquet, Jessica, Duca, Laurent, Romier, Béatrice, Maurice, Pascal, Debelle, Laurent, Martiny, Laurent, Durlach, Vincent, Baud, Stéphanie, Blaise, Sébastien |
| المساهمون: | Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), Nutrition, obésité et risque thrombotique (NORT), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Signalisation et Récepteurs Matriciels (SiRMa), Université de Reims Champagne-Ardenne (URCA)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS)-Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | ISSN: 2045-2322. |
| بيانات النشر: | HAL CCSD Nature Publishing Group |
| سنة النشر: | 2016 |
| المجموعة: | Université de Toulon: HAL |
| مصطلحات موضوعية: | [SDV]Life Sciences [q-bio] |
| الوصف: | International audience ; Sialic acids (SA) are monosaccharides that can be located at the terminal position of glycan chains on a wide range of proteins. The post-translational modifications, such as N-glycan chains, are fundamental to protein functions. Indeed, the hydrolysis of SA by specific enzymes such as neuraminidases can lead to drastic modifications of protein behavior. However, the relationship between desialylation of N-glycan chains and possible alterations of receptor function remains unexplored. Thus, the aim of the present study is to establish the impact of SA removal from N-glycan chains on their conformational behavior. We therefore undertook an in silico investigation using molecular dynamics to predict the structure of an isolated glycan chain. We performed, for the first time, 3 independent 500 ns simulations on bi-antennary and tri-antennary glycan chains displaying or lacking SA. We show that desialylation alters both the preferential conformation and the flexibility of the glycan chain. This study suggests that the behavior of glycan chains induced by presence or absence of SA may explain the changes in the protein function. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | hal-02347497; https://hal.science/hal-02347497; https://hal.science/hal-02347497/document; https://hal.science/hal-02347497/file/2016-04.pdf |
| DOI: | 10.1038/srep35666 |
| الاتاحة: | https://hal.science/hal-02347497 https://hal.science/hal-02347497/document https://hal.science/hal-02347497/file/2016-04.pdf https://doi.org/10.1038/srep35666 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.7A7D112E |
| قاعدة البيانات: | BASE |
| DOI: | 10.1038/srep35666 |
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