Channel Blockers Acting atN-Methyl-d-aspartate Receptors: Differential Effects of Mutations in the Vestibule and Ion Channel Pore

2002 ◽  
Vol 61 (3) ◽  
pp. 533-545 ◽  
Author(s):  
Keiko Kashiwagi ◽  
Takashi Masuko ◽  
Christopher D. Nguyen ◽  
Tomoko Kuno ◽  
Ikuko Tanaka ◽  
...  
Keyword(s):  
Ion Channel ◽  
Channel Blockers ◽  
Channel Pore ◽  
Differential Effects ◽  
Ion Channel Pore

scholarly journals Piezo1 ion channel pore properties are dictated by C-terminal region

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Bertrand Coste ◽  
Swetha E. Murthy ◽  
Jayanti Mathur ◽  
Manuela Schmidt ◽  
Yasmine Mechioukhi ◽  
...  
Keyword(s):  
Ion Channel ◽  
Terminal Region ◽  
Channel Pore ◽  
Ion Channel Pore ◽  
Pore Properties

scholarly journals Barbiturates Bind in the GLIC Ion Channel Pore and Cause Inhibition by Stabilizing a Closed State

2016 ◽  
Vol 292 (5) ◽  
pp. 1550-1558 ◽  
Author(s):  
Zaineb Fourati ◽  
Reinis Reinholds Ruza ◽  
Duncan Laverty ◽  
Emmanuelle Drège ◽  
Sandrine Delarue-Cochin ◽  
...  
Keyword(s):  
Ion Channel ◽  
Channel Pore ◽  
Closed State ◽  
Ion Channel Pore

scholarly journals IKS Ion-Channel Pore Conductance Can Result from Individual Voltage Sensor Movements

2020 ◽  
Vol 118 (3) ◽  
pp. 332a
Author(s):  
David Fedida ◽  
Maartje F. Westhoff ◽  
Jodene R. Eldstrom ◽  
Christopher I. Murray ◽  
Emely Thompson
Keyword(s):  
Ion Channel ◽  
Voltage Sensor ◽  
Channel Pore ◽  
Ion Channel Pore

scholarly journals Binding of κ-Conotoxin PVIIA to Shaker K+ Channels Reveals Different K+ and Rb+ Occupancies within the Ion Channel Pore

2004 ◽  
Vol 124 (1) ◽  
pp. 71-81 ◽  
Author(s):  
Anna Boccaccio ◽  
Franco Conti ◽  
Baldomero M. Olivera ◽  
Heinrich Terlau
Keyword(s):  
Ion Channel ◽  
Open Channel ◽  
K Channel ◽  
Closed Channel ◽  
Channel Pore ◽  
K Channels ◽  
Ion Channel Pore ◽  
Structural Work ◽  
High K ◽  
Insight Into

The x-ray structure of the KcsA channel at different [K+] and [Rb+] provided insight into how K+ channels might achieve high selectivity and high K+ transit rates and showed marked differences between the occupancies of the two ions within the ion channel pore. In this study, the binding of κ-conotoxin PVIIA (κ-PVIIA) to Shaker K+ channel in the presence of K+ and Rb+ was investigated. It is demonstrated that the complex results obtained were largely rationalized by differences in selectivity filter occupancy of this 6TM channels as predicted from the structural work on KcsA. κ-PVIIA inhibition of the Shaker K+ channel differs in the closed and open state. When K+ is the only permeant ion, increasing extracellular [K+] decreases κ-PVIIA affinity for closed channels by decreasing the “on” binding rate, but has no effect on the block of open channels, which is influenced only by the intracellular [K+]. In contrast, extracellular [Rb+] affects both closed- and open-channel binding. As extracellular [Rb+] increases, (a) binding to the closed channel is slightly destabilized and acquires faster kinetics, and (b) open channel block is also destabilized and the lowest block seems to occur when the pore is likely filled only by Rb+. These results suggest that the nature of the permeant ions determines both the occupancy and the location of the pore site from which they interact with κ-PVIIA binding. Thus, our results suggest that the permeant ion(s) within a channel pore can determine its functional and pharmacological properties.

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