1w33 | pdb_00001w33

BbCRASP-1 from Borrelia Burgdorferi

spinqualitylabelsall models 1w33, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1w33 is a 2 chain structure with sequence from Borbz. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. A novel fold for the factor H-binding protein BbCRASP-1 of Borrelia burgdorferi.,Cordes FS, Roversi P, Kraiczy P, Simon MM, Brade V, Jahraus O, Wallis R, Skerka C, Zipfel PF, Wallich R, Lea SM Nat Struct Mol Biol. 2005 Mar;12(3):276-7. Epub 2005 Feb 13. PMID:15711564 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Complement Regulator-Acquiring Surface Protein Complement regulator-acquiring surface protein

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