Modeling ion permeation through a bacterial voltage-gated calcium channel CaVAb using molecular dynamics simulations

2017 ◽  
Vol 13 (1) ◽  
pp. 208-214 ◽  
Author(s):  
Jamal Adiban ◽  
Yousef Jamali ◽  
Hashem Rafii-Tabar
Keyword(s):  
Molecular Dynamics ◽  
Calcium Channels ◽  
Calcium Channel ◽  
Molecular Dynamics Simulations ◽  
Selectivity Filter ◽  
Ion Permeation ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
Voltage Gated Calcium Channel ◽  
Dynamics Simulations

Ca2+ion binds tightly to the center of the selectivity filter of voltage-gated calcium channels.

scholarly journals Voltage-gated calcium channel blockers for psychiatric disorders: genomic reappraisal

2019 ◽  
Vol 216 (5) ◽  
pp. 250-253 ◽  
Author(s):  
Paul J. Harrison ◽  
Elizabeth M. Tunbridge ◽  
Annette C. Dolphin ◽  
Jeremy Hall
Keyword(s):  
Calcium Channels ◽  
Calcium Channel ◽  
Psychiatric Disorders ◽  
Calcium Channel Blockers ◽  
Channel Blockers ◽  
Risk Genes ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
Voltage Gated Calcium Channel ◽  
Second Use

SummaryWe reappraise the psychiatric potential of calcium channel blockers (CCBs). First, voltage-gated calcium channels are risk genes for several disorders. Second, use of CCBs is associated with altered psychiatric risks and outcomes. Third, research shows there is an opportunity for brain-selective CCBs, which are better suited to psychiatric indications.

scholarly journals A Selectivity Filter Gate Controls Voltage-Gated Calcium Channel Calcium-Dependent Inactivation

Neuron ◽  
2019 ◽  
Vol 101 (6) ◽  
pp. 1134-1149.e3 ◽  
Author(s):  
Fayal Abderemane-Ali ◽  
Felix Findeisen ◽  
Nathan D. Rossen ◽  
Daniel L. Minor
Keyword(s):  
Calcium Channel ◽  
Selectivity Filter ◽  
Voltage Gated ◽  
Calcium Dependent ◽  
Dependent Inactivation ◽  
Voltage Gated Calcium Channel

scholarly journals Disruption of the Key Ca2+ Binding Site in the Selectivity Filter of Neuronal Voltage-Gated Calcium Channels Inhibits Channel Trafficking

Cell Reports ◽  
2019 ◽  
Vol 29 (1) ◽  
pp. 22-33.e5 ◽  
Author(s):  
James O. Meyer ◽  
Shehrazade Dahimene ◽  
Karen M. Page ◽  
Laurent Ferron ◽  
Ivan Kadurin ◽  
...  
Keyword(s):  
Calcium Channels ◽  
Binding Site ◽  
Selectivity Filter ◽  
Channel Trafficking ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels

Determination of the charge profile in the KcsA selectivity filter using ab initio calculations and molecular dynamics simulations

2009 ◽  
Vol 11 (38) ◽  
pp. 8606 ◽  
Author(s):  
Sebastian Kraszewski ◽  
Céline Boiteux ◽  
Christophe Ramseyer ◽  
Claude Girardet
Keyword(s):  
Molecular Dynamics ◽  
Ab Initio Calculations ◽  
Ab Initio ◽  
Molecular Dynamics Simulations ◽  
Selectivity Filter ◽  
Dynamics Simulations

scholarly journals Thermodynamic coupling between activation and inactivation gating in potassium channels revealed by free energy molecular dynamics simulations

2011 ◽  
Vol 138 (6) ◽  
pp. 571-580 ◽  
Author(s):  
Albert C. Pan ◽  
Luis G. Cuello ◽  
Eduardo Perozo ◽  
Benoît Roux
Keyword(s):  
Molecular Dynamics ◽  
Free Energy ◽  
Molecular Dynamics Simulations ◽  
Conformational Changes ◽  
Ionic Current ◽  
Selectivity Filter ◽  
Recent Analysis ◽  
Steric Interaction ◽  
Inactivation Gating ◽  
Dynamics Simulations

The amount of ionic current flowing through K+ channels is determined by the interplay between two separate time-dependent processes: activation and inactivation gating. Activation is concerned with the stimulus-dependent opening of the main intracellular gate, whereas inactivation is a spontaneous conformational transition of the selectivity filter toward a nonconductive state occurring on a variety of timescales. A recent analysis of multiple x-ray structures of open and partially open KcsA channels revealed the mechanism by which movements of the inner activation gate, formed by the inner helices from the four subunits of the pore domain, bias the conformational changes at the selectivity filter toward a nonconductive inactivated state. This analysis highlighted the important role of Phe103, a residue located along the inner helix, near the hinge position associated with the opening of the intracellular gate. In the present study, we use free energy perturbation molecular dynamics simulations (FEP/MD) to quantitatively elucidate the thermodynamic basis for the coupling between the intracellular gate and the selectivity filter. The results of the FEP/MD calculations are in good agreement with experiments, and further analysis of the repulsive, van der Waals dispersive, and electrostatic free energy contributions reveals that the energetic basis underlying the absence of inactivation in the F103A mutation in KcsA is the absence of the unfavorable steric interaction occurring with the large Ile100 side chain in a neighboring subunit when the intracellular gate is open and the selectivity filter is in a conductive conformation. Macroscopic current analysis shows that the I100A mutant indeed relieves inactivation in KcsA, but to a lesser extent than the F103A mutant.

scholarly journals In-Silico Electrophysiology: On the Activation of Voltage-Gated Ion Channels using Molecular Dynamics Simulations

2016 ◽  
Vol 110 (3) ◽  
pp. 107a ◽  
Author(s):  
Mounir Tarek ◽  
Lucie Delemotte ◽  
Marina Kasimova ◽  
Michael L. Klein ◽  
Vincenzo Carnevale
Keyword(s):  
Molecular Dynamics ◽  
Ion Channels ◽  
Molecular Dynamics Simulations ◽  
In Silico ◽  
Voltage Gated ◽  
Voltage Gated Ion Channels ◽  
Dynamics Simulations ◽  
Gated Ion Channels
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