Computational Study of Binding of µ-Conotoxin GIIIA to Bacterial Sodium Channels Na<inf>V</inf>Ab and Na<inf>V</inf>Rh
MetadataShow full item record
© 2016 American Chemical Society. Structures of several voltage-gated sodium (Na V ) channels from bacteria have been determined recently, but the same feat might not be achieved for the mammalian counterparts in the near future. Thus, at present, computational studies of the mammalian Na V channels have to be performed using homology models based on the bacterial crystal structures. A successful homology model for the mammalian Na V 1.4 channel was recently constructed using the extensive mutation data for binding of µ-conotoxin GIIIA to Na V 1.4, which was further validated through studies of binding of other µ-conotoxins and ion permeation. Understanding the similarities and differences between the bacterial and mammalian Na V channels is an important issue, and the Na V 1.4-GIIIA system provides a good opportunity for such a comparison. To this end, we study the binding of GIIIA to the bacterial channels Na V Ab and Na V Rh. The complex structures are obtained using docking and molecular dynamics simulations, and the dissociation of GIIIA is studied through umbrella sampling simulations. The results are compared to those obtained from the Na V 1.4-GIIIA system, and the differences in the binding modes arising from the changes in the selectivity filters are highlighted.
Showing items related by title, author, creator and subject.
Martinac, B.; Nomura, T.; Chi, G.; Petrov, E.; Rohde, P.; Battle, A.; Foo, A.; Constantine, M.; Rothnagel, R.; Carne, S.; Deplazes, Evelyne; Cornell, B.; Cranfield, C.; Hankamer, B.; Landsberg, M. (2014)Significance: Sensations of touch and hearing are manifestations of mechanical contact and air pressure acting on touch receptors and hair cells of the inner ear, respectively. In bacteria, osmotic pressure exerts a ...
Interaction of tarantula venom peptide ProTx-II with lipid membranes is a prerequisite for its inhibition of human voltage-gated sodium channel NaV 1.7Henriques, S.; Deplazes, Evelyne; Lawrence, N.; Cheneval, O.; Chaousis, S.; Inserra, M.; Thongyoo, P.; King, G.; Mark, A.; Vetter, I.; Craik, D.; Schroeder, C. (2016)ProTx-II is a disulfide-rich peptide toxin from tarantula venom able to inhibit the human voltage-gated sodium channel 1.7 (hNaV 1.7), a channel reported to be involved in nociception, and thus it might have potential as ...
Modelling the co-occurence of Streptococcus pneumoniae with other bacterial and viral pathogens in the upper respiratory tractJacoby, P.; Watson, K.; Bowman, J.; Taylor, A.; Riley, T.; Smith, D.; Lehmann, Deborah (2007)Go to ScienceDirect® Home Skip Main Navigation Links Brought to you by: The University of Western Australia Library Login: + Register Athens/Institution Login Not Registered? - User Name: Password: ...