TY - JOUR T1 - Profiles of ILY, VLY and Sm-hPAF Interaction with Human CD59 JF - Anticancer Research JO - Anticancer Res SP - 2901 LP - 2904 VL - 33 IS - 7 AU - YUKI KAWAGUCHI AU - ATSUSHI TABATA AU - HIDEAKI NAGAMUNE AU - KAZUTO OHKURA Y1 - 2013/07/01 UR - http://ar.iiarjournals.org/content/33/7/2901.abstract N2 - Background: 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. Materials and Methods: 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. Results: 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. Conclusion: A hydrogen bond (ILY Arg432–hCD59 Glu76) was observed between ILY and hCD59, and a stronger interaction was formed by flexible adjustment between them. ER -