Faculty of Pharmaceutical Sciences, Suzuka University of Medical Science, 3500-3 Minamitamagaki-cho, Suzuka, Mie 513-8670, Japan.
Anticancer Res. 2013 Jul;33(7):2901-4.
The molecular features of a new member of the bacterially -derived cytolysin family were examined. In particular, the interactive mechanisms of intermedilysin (ILY), vaginolysin (VLY), and Streptococcus mitis-derived human platelet aggregation factor (Sm-hPAF) with human CD59 (hCD59) were analyzed.
Molecular models of VLY and Sm-hPAF were constructed based on X-ray data of ILY (protein data bank ID=1S3R), and their interactive profiles with hCD59 were examined using molecular simulation.
Non-binding (NB) energy between ILY and hCD59 was three orders of magnitude higher than the energy between VLY and hCD59. NB energy between Sm-hPAF and hCD59 was similar to that between VLY and hCD59.
A hydrogen bond (ILY Arg432-hCD59 Glu76) was observed between ILY and hCD59, and a stronger interaction was formed by flexible adjustment between them.
研究了一种新的细菌衍生细胞毒素家族成员的分子特征。特别分析了中介素（ILY）、阴道溶素（VLY）和来源于链球菌的人血小板聚集因子（Sm-hPAF）与人类 CD59（hCD59）的相互作用机制。
根据 ILY（蛋白质数据库 ID=1S3R）的 X 射线数据构建了 VLY 和 Sm-hPAF 的分子模型，并使用分子模拟研究了它们与 hCD59 的相互作用模式。
ILY 与 hCD59 之间的非结合（NB）能量比 VLY 与 hCD59 之间的能量高三个数量级。Sm-hPAF 与 hCD59 之间的 NB 能量与 VLY 与 hCD59 之间的 NB 能量相似。
ILY 与 hCD59 之间观察到氢键（ILY Arg432-hCD59 Glu76），通过它们之间的灵活调节形成了更强的相互作用。
