Description

Structural mechanisms behind variations in glycosaminoglycan (GAG) affinities of decorin-binding protein As (DBPAs) from different Borrelia strains were investigated using NMR. DBPA from strain PBr was revealed to have an additional GAG-binding epitope and a retracted linker allowing more access to its GAG-binding sites.

Downloads
PDF (1.5 MB)

Details

Title
  • Structural Mechanisms Underlying Sequence-Dependent Variations in GAG Affinities of Decorin Binding Protein A, a Borrelia Burgdorferi Adhesin
Contributors
Date Created
2015-05-01
Resource Type
  • Text
  • Collections this item is in
    Identifier
    • Digital object identifier: 10.1042/BJ20141201
    • Identifier Type
      International standard serial number
      Identifier Value
      0264-6021
    • Identifier Type
      International standard serial number
      Identifier Value
      1470-8728

    Citation and reuse

    Cite this item

    This is a suggested citation. Consult the appropriate style guide for specific citation guidelines.

    Morgan, Ashli M., & Wang, Xu (2015). Structural mechanisms underlying sequence-dependent variations in GAG affinities of decorin binding protein A, a Borrelia burgdorferi adhesin. BIOCHEMICAL JOURNAL, 467, 439-451. http://dx.doi.org/10.1042/BJ20141201

    Machine-readable links