1w33

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w33 OCA], [http://www.ebi.ac.uk/pdbsum/1w33 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w33 RCSB]</span>
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[[Category: Wallich, R.]]
[[Category: Wallich, R.]]
[[Category: Zipfel, P.]]
[[Category: Zipfel, P.]]
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[[Category: GOL]]
 
[[Category: complement regulator acquiring surface protein]]
[[Category: complement regulator acquiring surface protein]]
[[Category: factor h binding]]
[[Category: factor h binding]]
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[[Category: tick]]
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Revision as of 21:30, 30 March 2008


PDB ID 1w33

Drag the structure with the mouse to rotate
, resolution 2.7Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



BBCRASP-1 FROM BORRELIA BURGDORFERI


Overview

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.

About this Structure

1W33 is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.

Reference

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

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