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    Restricted N-glycan Conformational Space in the PDB and Its Implication in Glycan Structure Modeling

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    Issue Date
    2013-03-14
    Author
    Jo, Sunhwan
    Lee, Hui Sun
    Skolnick, Jeffrey
    Im, Wonpil
    Publisher
    Public Library of Science
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Rights
    Copyright ©2013 Jo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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    Abstract
    Understanding glycan structure and dynamics is central to understanding protein-carbohydrate recognition and its role in protein-protein interactions. Given the difficulties in obtaining the glycan's crystal structure in glycoconjugates due to its flexibility and heterogeneity, computational modeling could play an important role in providing glycosylated protein structure models. To address if glycan structures available in the PDB can be used as templates or fragments for glycan modeling, we present a survey of the N-glycan structures of 35 different sequences in the PDB. Our statistical analysis shows that the N-glycan structures found on homologous glycoproteins are significantly conserved compared to the random background, suggesting that N-glycan chains can be confidently modeled with template glycan structures whose parent glycoproteins share sequence similarity. On the other hand, N-glycan structures found on non-homologous glycoproteins do not show significant global structural similarity. Nonetheless, the internal substructures of these N-glycans, particularly, the substructures that are closer to the protein, show significantly similar structures, suggesting that such substructures can be used as fragments in glycan modeling. Increased interactions with protein might be responsible for the restricted conformational space of N-glycan chains. Our results suggest that structure prediction/modeling of N-glycans of glycoconjugates using structure database could be effective and different modeling approaches would be needed depending on the availability of template structures.
    Description
    A grant from the One-University Open Access Fund at the University of Kansas was used to defray the author’s publication fees in this Open Access journal. The Open Access Fund, administered by librarians from the KU, KU Law, and KUMC libraries, is made possible by contributions from the offices of KU Provost, KU Vice Chancellor for Research & Graduate Studies, and KUMC Vice Chancellor for Research. For more information about the Open Access Fund, please see http://library.kumc.edu/authors-fund.xml.
    URI
    http://hdl.handle.net/1808/11539
    DOI
    https://doi.org/10.1371/journal.pcbi.1002946
    Collections
    • Molecular Biosciences Scholarly Works [573]
    • KU Scholarly Papers Funded by the KU Open Access Fund [202]
    Citation
    Im, Wonpil; et al. (2013) Restricted N-glycan Conformational Space in the PDB and Its Implication in Glycan Structure Modeling. Plos Computational Biology, 9.3: 1-10. http://dx.doi.org/10.1371/journal.pcbi.1002946

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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