| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3422331 | Trends in Microbiology | 2008 | 4 Pages |
Abstract
Several receptors have been described for the Helicobacter pylori vacuolating toxin VacA, which exerts different effects on epithelial cells and on immune cells. The crystal structure of the putative receptor-binding domain of VacA (p55) has now been solved. It consists of a parallel β-helix with a C-terminal globular domain. A comparison between allelic variants of p55 and docking of the p55 domain into the quaternary structure, as shown by electron microscopy, revealed structural features that might be important for elucidating the molecular details of receptor interaction and channel formation.
Related Topics
Life Sciences
Immunology and Microbiology
Microbiology
Authors
Xaver Sewald, Wolfgang Fischer, Rainer Haas,