Title : Structural mechanisms underlying sequence-dependent variations in GAG affinities of decorin binding protein A, a Borrelia burgdorferi adhesin.

Pub. Date : 2015 May 1

PMID : 25695518






6 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 DBPA facilitates the bacteria"s colonization of human tissue by adhering to glycosaminoglycan (GAG), a sulfated polysaccharide. Glycosaminoglycans Y-box binding protein 3 Homo sapiens
2 DBPA facilitates the bacteria"s colonization of human tissue by adhering to glycosaminoglycan (GAG), a sulfated polysaccharide. Glycosaminoglycans Y-box binding protein 3 Homo sapiens
3 Interestingly, DBPA sequence variation among different strains of Borrelia spirochetes is high, resulting in significant differences in their GAG affinities. Glycosaminoglycans Y-box binding protein 3 Homo sapiens
4 In particular, the C-terminus of PBr DBPA, unlike C-termini from B31 and N40 DBPAs, is positioned away from the GAG-binding pocket and the linker between helices one and two of PBr DBPA is highly structured and retracted from the GAG-binding pocket. Glycosaminoglycans Y-box binding protein 3 Homo sapiens
5 In particular, the C-terminus of PBr DBPA, unlike C-termini from B31 and N40 DBPAs, is positioned away from the GAG-binding pocket and the linker between helices one and two of PBr DBPA is highly structured and retracted from the GAG-binding pocket. Glycosaminoglycans Y-box binding protein 3 Homo sapiens
6 The repositioning of the C-terminus allowed the formation of an extra GAG-binding epitope in PBr DBPA and the retracted linker gave GAG ligands more access to the GAG-binding epitopes than other DBPAs. Glycosaminoglycans Y-box binding protein 3 Homo sapiens