scholarly journals Structural Basis for the Modulation of the Neuronal Voltage-Gated Sodium Channel NaV1.6 by Calmodulin

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Vishnu Priyanka Reddy Chichili ◽  
Yucheng Xiao ◽  
J. Seetharaman ◽  
Theodore R. Cummins ◽  
J. Sivaraman
Keyword(s):  
Sodium Channel ◽  
Structural Basis ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated

scholarly journals Assessing the Structural Basis of μ-Conotoxin KIIIA Inhibition of the Voltage-Gated Sodium Channel Nav1.7

2018 ◽  
Vol 114 (3) ◽  
pp. 635a ◽  
Author(s):  
Ian H. Kimball ◽  
Phuong T. Nguyen ◽  
Jon T. Sack ◽  
Vladimir Yarov-Yarovoy
Keyword(s):  
Sodium Channel ◽  
Structural Basis ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated

scholarly journals Structures of closed and open states of a voltage-gated sodium channel

2017 ◽  
Vol 114 (15) ◽  
pp. E3051-E3060 ◽  
Author(s):  
Michael J. Lenaeus ◽  
Tamer M. Gamal El-Din ◽  
Christopher Ing ◽  
Karthik Ramanadane ◽  
Régis Pomès ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Full Range ◽  
Structural Basis ◽  
Ion Permeation ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Gating Mechanism ◽  
Activation Gate ◽  
Open States

Bacterial voltage-gated sodium channels (BacNavs) serve as models of their vertebrate counterparts. BacNavs contain conserved voltage-sensing and pore-forming domains, but they are homotetramers of four identical subunits, rather than pseudotetramers of four homologous domains. Here, we present structures of two NaVAb mutants that capture tightly closed and open states at a resolution of 2.8–3.2 Å. Introduction of two humanizing mutations in the S6 segment (NaVAb/FY: T206F and V213Y) generates a persistently closed form of the activation gate in which the intracellular ends of the four S6 segments are drawn tightly together to block ion permeation completely. This construct also revealed the complete structure of the four-helix bundle that forms the C-terminal domain. In contrast, truncation of the C-terminal 40 residues in NavAb/1–226 captures the activation gate in an open conformation, revealing the open state of a BacNav with intact voltage sensors. Comparing these structures illustrates the full range of motion of the activation gate, from closed with its orifice fully occluded to open with an orifice of ∼10 Å. Molecular dynamics and free-energy simulations confirm designation of NaVAb/1–226 as an open state that allows permeation of hydrated Na+, and these results also support a hydrophobic gating mechanism for control of ion permeation. These two structures allow completion of a closed–open–inactivated conformational cycle in a single voltage-gated sodium channel and give insight into the structural basis for state-dependent binding of sodium channel-blocking drugs.

scholarly journals On the structural basis for ionic selectivity among Na+, K+, and Ca2+ in the voltage-gated sodium channel

1996 ◽  
Vol 71 (6) ◽  
pp. 3110-3125 ◽  
Author(s):  
I. Favre ◽  
E. Moczydlowski ◽  
L. Schild
Keyword(s):  
Sodium Channel ◽  
Structural Basis ◽  
Ionic Selectivity ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated

The Voltage-Gated Sodium Channel Nav1.2 Contributes to Neurodegeneration in an Animal Model of Multiple Sclerosis

2016 ◽  
Vol 47 (S 01) ◽  
Author(s):  
W. Fazeli ◽  
B. Schattling ◽  
B. Engeland ◽  
M. Friese ◽  
D. Isbrand
Keyword(s):  
Multiple Sclerosis ◽  
Animal Model ◽  
Sodium Channel ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated

Isoform Selective Voltage-Gated Sodium Channel Modulators and the Therapy of Pain

2013 ◽  
Vol 21 (2) ◽  
pp. 164-186 ◽  
Author(s):  
Marko Jukic ◽  
Danijel Kikelj ◽  
Marko Anderluh
Keyword(s):  
Sodium Channel ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Therapy Of Pain
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