| Literature DB >> 15711564 |
Frank S Cordes1, Pietro Roversi, Peter Kraiczy, Markus M Simon, Volker Brade, Oliver Jahraus, Russell Wallis, Christine Skerka, Peter F Zipfel, Reinhard Wallich, Susan M Lea.
Abstract
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.Entities:
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Year: 2005 PMID： 15711564 DOI： 10.1038/nsmb902
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369