| Literature DB >> 18280164 |
Xaver Sewald1, Wolfgang Fischer, Rainer Haas.
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 beta-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.Entities:
Mesh：
Substances：
Year: 2008 PMID： 18280164 DOI： 10.1016/j.tim.2008.01.001
Source DB: PubMed Journal: Trends Microbiol ISSN： 0966-842X Impact factor: 17.079