A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi
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...
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| Main Authors: | , , , , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
13 February 2005
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| In: |
Nature structural & molecular biology
Year: 2005, Volume: 12, Issue: 3, Pages: 276-277 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb902 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb902 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb902 |
| Author Notes: | Frank S. Cordes, Pietro Roversi, Peter Kraiczy, Markus M. Simon, Volker Brade, Oliver Jahraus, Russell Wallis, Christine Skerka, Peter F. Zipfel, Reinhard Wallich & Susan M. Lea |
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| 520 | |a 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. | ||
| 650 | 4 | |a Bacterial Proteins | |
| 650 | 4 | |a Blood Proteins | |
| 650 | 4 | |a Complement C3b Inactivator Proteins | |
| 650 | 4 | |a Complement Factor H | |
| 650 | 4 | |a Dimerization | |
| 650 | 4 | |a Lyme Disease | |
| 650 | 4 | |a Membrane Proteins | |
| 650 | 4 | |a Protein Folding | |
| 650 | 4 | |a Protein Structure, Secondary | |
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| 700 | 1 | |a Lea, Susan M. |e VerfasserIn |4 aut | |
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