University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Surgery (Austin & Northern Health)
  • Surgery (Austin & Northern Health) - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Surgery (Austin & Northern Health)
  • Surgery (Austin & Northern Health) - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Molecular Simulations of Carbohydrates with a Fucose-Binding Burkholderia ambifaria Lectin Suggest Modulation by Surface Residues Outside the Fucose-Binding Pocket

    Thumbnail
    Download
    published version (4.669Mb)

    Citations
    Scopus
    Web of Science
    Altmetric
    2
    4
    Author
    Dingjan, T; Imberty, A; Perez, S; Yuriev, E; Ramsland, PA
    Date
    2017-06-21
    Source Title
    Frontiers in Pharmacology
    Publisher
    FRONTIERS MEDIA SA
    University of Melbourne Author/s
    Ramsland, Paul
    Affiliation
    Surgery (Austin & Northern Health)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Dingjan, T., Imberty, A., Perez, S., Yuriev, E. & Ramsland, P. A. (2017). Molecular Simulations of Carbohydrates with a Fucose-Binding Burkholderia ambifaria Lectin Suggest Modulation by Surface Residues Outside the Fucose-Binding Pocket. FRONTIERS IN PHARMACOLOGY, 8 (JUN), https://doi.org/10.3389/fphar.2017.00393.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/256374
    DOI
    10.3389/fphar.2017.00393
    Abstract
    Burkholderia ambifaria is an opportunistic respiratory pathogen belonging to the Burkholderia cepacia complex, a collection of species responsible for the rapidly fatal cepacia syndrome in cystic fibrosis patients. A fucose-binding lectin identified in the B. ambifaria genome, BambL, is able to adhere to lung tissue, and may play a role in respiratory infection. X-ray crystallography has revealed the bound complex structures for four fucosylated human blood group epitopes (blood group B, H type 1, H type 2, and Lex determinants). The present study employed computational approaches, including docking and molecular dynamics (MD), to extend the structural analysis of BambL-oligosaccharide complexes to include four additional blood group saccharides (A, Lea, Leb, and Ley) and a library of blood-group-related carbohydrates. Carbohydrate recognition is dominated by interactions with fucose via a hydrogen-bonding network involving Arg15, Glu26, Ala38, and Trp79 and a stacking interaction with Trp74. Additional hydrogen bonds to non-fucose residues are formed with Asp30, Tyr35, Thr36, and Trp74. BambL recognition is dominated by interactions with fucose, but also features interactions with other parts of the ligands that may modulate specificity or affinity. The detailed computational characterization of the BambL carbohydrate-binding site provides guidelines for the future design of lectin inhibitors.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [53102]
    • Surgery (Austin & Northern Health) - Research Publications [406]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors