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Borrelia burgdorferi, a spirochete transmitted to human hosts during feeding of infected Ixodes ticks, is the causative agent of Lyme disease. Serum-resistant B. burgdorferi strains cause a chronic, multisystemic form of the disease and bind complement factor H (FH) and FH-like protein 1 (FHL-1) on the spirochete surface. Here we report the atomic structure for the key FHL-1- and FH-binding protein BbCRASP-1 and reveal a homodimer that presents a novel target for drug design.

Original publication

DOI

10.1038/nsmb902

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

03/2005

Volume

12

Pages

276 - 277

Keywords

Bacterial Proteins, Blood Proteins, Complement C3b Inactivator Proteins, Complement Factor H, Dimerization, Lyme Disease, Membrane Proteins, Protein Folding, Protein Structure, Secondary