Sewald Xaver, Fischer Wolfgang, Haas Rainer
Max von Pettenkofer-Institute for Hygiene and Medical Microbiology, Ludwig-Maximilians-University, Pettenkoferstrasse 9a, D-80336 Munich, Germany.
Trends Microbiol. 2008 Mar;16(3):89-92. doi: 10.1016/j.tim.2008.01.001. Epub 2008 Feb 14.
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.
幽门螺杆菌空泡毒素VacA已被描述有几种受体，该毒素对上皮细胞和免疫细胞有不同作用。VacA假定受体结合域（p55）的晶体结构现已解析。它由一个带有C端球状结构域的平行β-螺旋组成。p55等位基因变体之间的比较以及如电子显微镜所示将p55结构域对接至四级结构，揭示了可能对阐明受体相互作用和通道形成的分子细节很重要的结构特征。
