Abstract
Equinatoxin II (EqtII) is a 179-residue toxin from the venom of the sea anemone Actinia equina. EqtII is a member of the actinoporin family of proteins, which have potent lytic activity towards membranes containing sphingomyelin (SM). To gain insight into the atomic-level details governing SM selectivity, a series of all-atom molecular dynamics simulations were performed to model the binding of EqtII to micelles of n-dodecylphosphocholine (DPC) and DPC/SM. These models are in good agreement with concurrent high-resolution solution NMR studies and prior data [1, 2] that suggests membrane binding is dependent on a conserved cluster of aromatic amino acids. From this groundwork study, further simulations will be performed to investigate EqtII oligomerisation and membrane insertion to determine the mechanism of pore formation.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
