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.
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Title
- Structural Mechanisms Underlying Sequence-Dependent Variations in GAG Affinities of Decorin Binding Protein A, a Borrelia Burgdorferi Adhesin
Contributors
- Morgan, Ashli (Author)
- Wang, Xu (Author)
- Department of Chemistry and Biochemistry (Contributor)
Date Created
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2015-05-01
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Identifier
- Digital object identifier: 10.1042/BJ20141201
- Identifier TypeInternational standard serial numberIdentifier Value0264-6021
- Identifier TypeInternational standard serial numberIdentifier Value1470-8728
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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