McNicholas, Stuart and Agirre, Jon orcid.org/0000-0002-1086-0253 (2017) Glycoblocks:a schematic three-dimensional representation for glycans and their interactions. Acta crystallographica. Section D, Structural biology. pp. 187-194. ISSN 2059-7983
Abstract
The close-range interactions provided by covalently linked glycans are essential for the correct folding of glycoproteins and also play a pivotal role in recognition processes. Being able to visualise protein-glycan and glycan-glycan contacts in a clear way is thus of great importance for the understanding of these biological processes. In structural terms, glycosylation sugars glue the protein together via hydrogen bonds, whereas non-covalently bound glycans frequently harness additional stacking interactions. Finding an unobscured molecular view of these multipartite scenarios is usually far from trivial; in addition to the need to show the interacting protein residues, glycans may contain many branched sugars, each composed of more than ten non-H atoms and offering more than three potential bonding partners. With structural glycoscience finally gaining popularity and steadily increasing the deposition rate of three-dimensional structures of glycoproteins, the need for a clear way of depicting these interactions is more pressing than ever. Here a schematic representation, named Glycoblocks, is introduced which combines a simplified bonding-network depiction (covering hydrogen bonds and stacking interactions) with the familiar two-dimensional glycan notation used by the glycobiology community, brought into three dimensions by the CCP4 molecular graphics project (CCP4mg).
Metadata
Item Type: | Article |
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Authors/Creators: |
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Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 21 Feb 2017 14:20 |
Last Modified: | 16 Oct 2024 13:35 |
Published Version: | https://doi.org/10.1107/S2059798316013553 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1107/S2059798316013553 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:112642 |