Dissecting the actinoporin pore-forming mechanism.
Crystal structures of the eukaryotic pore-forming toxin sticholysin II, its complex with phosphocholine, and electron microscopy of 2D crystals on lipid monolayer give insights into the sequential steps of the actinoporin membrane penetration.
Anderluh
Gregor
G
Department of Biology, Biotechnical Faculty, University of Ljubljana, Vecna pot 111, 1000 Ljubljana, Slovenia.
Macek
Peter
P
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D003064:Cnidarian Venoms / Q000737:chemistry; D018360:Crystallography, X-Ray; D006460:Hemolysin Proteins / Q000737:chemistry; D008055:Lipids / Q000737:chemistry; D021962:Membrane Microdomains / Q000737:chemistry; D008854:Microscopy, Electron; D009842:Oligopeptides / Q000737:chemistry; D010767:Phosphorylcholine / Q000737:chemistry; D018272:Porins / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012615:Sea Anemones
D003064:Cnidarian Venoms; D006460:Hemolysin Proteins; D008055:Lipids; D009842:Oligopeptides; D018272:Porins; C404794:sticholysin II; D010767:Phosphorylcholine; C047981:arginyl-glycyl-aspartic acid