scholarly journals The Tetrodotoxin Binding Site Is within the Outer Vestibule of the Sodium Channel

Marine Drugs ◽  
2010 ◽  
Vol 8 (2) ◽  
pp. 219-234 ◽  
Author(s):  
Harry A. Fozzard ◽  
Gregory M. Lipkind
Keyword(s):  
Sodium Channel ◽  
Binding Site ◽  
Outer Vestibule

Probing the Redox States of Sodium Channel Cysteines at the Binding Site of μO§-Conotoxin GVIIJ

Biochemistry ◽  
2015 ◽  
Vol 54 (25) ◽  
pp. 3911-3920 ◽  
Author(s):  
Min-Min Zhang ◽  
Joanna Gajewiak ◽  
Layla Azam ◽  
Grzegorz Bulaj ◽  
Baldomero M. Olivera ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Binding Site ◽  
Redox States

scholarly journals A mu-conotoxin-insensitive Na+ channel mutant: possible localization of a binding site at the outer vestibule

1995 ◽  
Vol 69 (5) ◽  
pp. 1657-1665 ◽  
Author(s):  
S.C. Dudley ◽  
H. Todt ◽  
G. Lipkind ◽  
H.A. Fozzard
Keyword(s):  
Binding Site ◽  
Na Channel ◽  
Outer Vestibule

scholarly journals Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7

2016 ◽  
Vol 291 (33) ◽  
pp. 17049-17065 ◽  
Author(s):  
Sónia Troeira Henriques ◽  
Evelyne Deplazes ◽  
Nicole Lawrence ◽  
Olivier Cheneval ◽  
Stephanie Chaousis ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Binding Site ◽  
Lipid Membranes ◽  
Lipid Membrane ◽  
Membrane Binding ◽  
Voltage Sensor ◽  
Resonance Fluorescence ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Voltage Sensor Domain

ProTx-II is a disulfide-rich peptide toxin from tarantula venom able to inhibit the human voltage-gated sodium channel 1.7 (hNaV1.7), a channel reported to be involved in nociception, and thus it might have potential as a pain therapeutic. ProTx-II acts by binding to the membrane-embedded voltage sensor domain of hNaV1.7, but the precise peptide channel-binding site and the importance of membrane binding on the inhibitory activity of ProTx-II remain unknown. In this study, we examined the structure and membrane-binding properties of ProTx-II and several analogues using NMR spectroscopy, surface plasmon resonance, fluorescence spectroscopy, and molecular dynamics simulations. Our results show a direct correlation between ProTx-II membrane binding affinity and its potency as an hNaV1.7 channel inhibitor. The data support a model whereby a hydrophobic patch on the ProTx-II surface anchors the molecule at the cell surface in a position that optimizes interaction of the peptide with the binding site on the voltage sensor domain. This is the first study to demonstrate that binding of ProTx-II to the lipid membrane is directly linked to its potency as an hNaV1.7 channel inhibitor.

Structural Features of the Binding Site for Diphenin and other Anticonvulsants belonging to the Group of Sodium Channel Blockers

2005 ◽  
Vol 39 (9) ◽  
pp. 488-496
Author(s):  
V. A. Frolovskii ◽  
Yu. N. Studnev ◽  
T. L. Garibova ◽  
I. P. Galaeva ◽  
V. A. Kraineva ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Binding Site ◽  
Structural Features ◽  
Channel Blockers ◽  
Sodium Channel Blockers
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