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‘Naked’ and Hydrated Conformers of the Conserved Core Pentasaccharide of N-linked Glycoproteins and Its Building Blocks
[Image: see text] N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit −Man(3)GlcNAc(2)– lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an ind...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901393/ https://www.ncbi.nlm.nih.gov/pubmed/24127839 http://dx.doi.org/10.1021/ja4056678 |
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author | Barry, Conor S. Cocinero, Emilio J. Çarçabal, Pierre Gamblin, David P. Stanca-Kaposta, E. Cristina Remmert, Sarah M. Fernández-Alonso, María C. Rudić, Svemir Simons, John P. Davis, Benjamin G. |
author_facet | Barry, Conor S. Cocinero, Emilio J. Çarçabal, Pierre Gamblin, David P. Stanca-Kaposta, E. Cristina Remmert, Sarah M. Fernández-Alonso, María C. Rudić, Svemir Simons, John P. Davis, Benjamin G. |
author_sort | Barry, Conor S. |
collection | PubMed |
description | [Image: see text] N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit −Man(3)GlcNAc(2)– 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. |
format | Online Article Text |
id | pubmed-3901393 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-39013932014-01-24 ‘Naked’ and Hydrated Conformers of the Conserved Core Pentasaccharide of N-linked Glycoproteins and Its Building Blocks Barry, Conor S. Cocinero, Emilio J. Çarçabal, Pierre Gamblin, David P. Stanca-Kaposta, E. Cristina Remmert, Sarah M. Fernández-Alonso, María C. Rudić, Svemir Simons, John P. Davis, Benjamin G. J Am Chem Soc [Image: see text] N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit −Man(3)GlcNAc(2)– 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. American Chemical Society 2013-10-15 2013-11-13 /pmc/articles/PMC3901393/ /pubmed/24127839 http://dx.doi.org/10.1021/ja4056678 Text en Copyright © 2013 American Chemical Society Terms of Use CC-BY (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) |
spellingShingle | Barry, Conor S. Cocinero, Emilio J. Çarçabal, Pierre Gamblin, David P. Stanca-Kaposta, E. Cristina Remmert, Sarah M. Fernández-Alonso, María C. Rudić, Svemir Simons, John P. Davis, Benjamin G. ‘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 |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3901393/ https://www.ncbi.nlm.nih.gov/pubmed/24127839 http://dx.doi.org/10.1021/ja4056678 |
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