'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks.
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, assoc...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2013
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| _version_ | 1826300655669608448 |
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| author | Barry, C Cocinero, E Carçabal, P Gamblin, D Stanca-Kaposta, E Remmert, S Fernández-Alonso, M Rudić, S Simons, J Davis, B |
| author_facet | Barry, C Cocinero, E Carçabal, P Gamblin, D Stanca-Kaposta, E Remmert, S Fernández-Alonso, M Rudić, S Simons, J Davis, B |
| author_sort | Barry, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T05:20:28Z |
| format | Journal article |
| id | oxford-uuid:deb689f8-542d-476a-ab7d-187710da96dc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:20:28Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | oxford-uuid:deb689f8-542d-476a-ab7d-187710da96dc2022-03-27T09:34:11Z'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:deb689f8-542d-476a-ab7d-187710da96dcEnglishSymplectic Elements at Oxford2013Barry, CCocinero, ECarçabal, PGamblin, DStanca-Kaposta, ERemmert, SFernández-Alonso, MRudić, SSimons, JDavis, BN-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. |
| spellingShingle | Barry, C Cocinero, E Carçabal, P Gamblin, D Stanca-Kaposta, E Remmert, S Fernández-Alonso, M Rudić, S Simons, J Davis, B 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title | 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title_full | 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title_fullStr | 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title_full_unstemmed | 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title_short | 'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks. |
| title_sort | naked and hydrated conformers of the conserved core pentasaccharide of n linked glycoproteins and its building blocks |
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