‘Naked’ and Hydrated Conformers of the Conserved Core Pentasaccharide of N-linked Glycoproteins and Its Building Blocks
| Autor: | John P. Simons, Pierre Çarçabal, Emilio J. Cocinero, E. Cristina Stanca-Kaposta, Conor S. Barry, María del Carmen Fernández-Alonso, David P. Gamblin, Svemir Rudić, Sarah M. Remmert, Benjamin G. Davis |
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| Rok vydání: | 2013 |
| Předmět: |
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Molecular Glycosylation Stereochemistry Molecular Sequence Data Oligosaccharides Branching (polymer chemistry) Biochemistry Article Catalysis chemistry.chemical_compound Colloid and Surface Chemistry Carbohydrate Conformation Side chain Asparagine Conformational isomerism Glycoproteins chemistry.chemical_classification Solvation General Chemistry Crystallography Carbohydrate Sequence chemistry Carbohydrate conformation Glycoprotein |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/ja4056678 |
| Popis: | N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit −Man3GlcNAc2– lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal −GlcNAc-GlcNAc– unit acts as a rigid rod, while the central, and unusual, −Man-β-1,4-GlcNAc– linkage is more flexible and is modulated by the distal Man-α-1,3– and Man-α-1,6– branching units. Solvation stiffens the ‘rod’ but leaves the distal residues flexible, through a β-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies. |
| Databáze: | OpenAIRE |
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