A Protein Chemical Approach to Channel Structure and Function: The Proton Channel of the Vacuolar H+ -ATPase

2008 ◽  
pp. 207-222 ◽  
Author(s):  
John B. C. Findlay ◽  
Michael A. Harrison
Keyword(s):  
Structure And Function ◽  
Channel Structure ◽  
Proton Channel ◽  
Chemical Approach ◽  
And Function

scholarly journals Insights into the structure and function of HV1 from a meta-analysis of mutation studies

2016 ◽  
Vol 148 (2) ◽  
pp. 97-118 ◽  
Author(s):  
Thomas E. DeCoursey ◽  
Deri Morgan ◽  
Boris Musset ◽  
Vladimir V. Cherny
Keyword(s):  
Amino Acid ◽  
Ion Channel ◽  
Meta Analysis ◽  
Structure And Function ◽  
Proton Channel ◽  
Vast Array ◽  
Voltage Gated ◽  
Interspecies Differences ◽  
And Function ◽  
Sheer Number

The voltage-gated proton channel (HV1) is a widely distributed, proton-specific ion channel with unique properties. Since 2006, when genes for HV1 were identified, a vast array of mutations have been generated and characterized. Accessing this potentially useful resource is hindered, however, by the sheer number of mutations and interspecies differences in amino acid numbering. This review organizes all existing information in a logical manner to allow swift identification of studies that have characterized any particular mutation. Although much can be gained from this meta-analysis, important questions about the inner workings of HV1 await future revelation.

Role of the C-Terminus of the High-Conductance Calcium-Activated Potassium Channel in Channel Structure and Function

Biochemistry ◽  
2005 ◽  
Vol 44 (30) ◽  
pp. 10135-10144 ◽  
Author(s):  
William A. Schmalhofer ◽  
Manuel Sanchez ◽  
Ge Dai ◽  
Ashvin Dewan ◽  
Lorena Secades ◽  
...  
Keyword(s):  
Potassium Channel ◽  
Structure And Function ◽  
Channel Structure ◽  
C Terminus ◽  
And Function ◽  
Calcium Activated Potassium Channel ◽  
High Conductance

scholarly journals Refinement of a Cryo-EM Structure of hERG: Bridging Structure and Function

2020 ◽  
Author(s):  
H.M. Khan ◽  
J. Guo ◽  
H.J. Duff ◽  
D. P. Tieleman ◽  
S. Y. Noskov
Keyword(s):  
Molecular Dynamics ◽  
High Resolution ◽  
Salt Bridge ◽  
Structure And Function ◽  
Channel Structure ◽  
Salt Bridges ◽  
Voltage Sensing ◽  
Chain Conformations ◽  
And Function ◽  
Voltage Sensing Domain

AbstractThe human ether-a-go-go-related gene (hERG) encodes the voltage gated potassium channel (KCNH2 or Kv11.1, commonly known as hERG). This channel plays a pivotal role in the stability of phase 3 repolarization of the cardiac action potential. Although a high-resolution cryo-EM structure is available for its depolarized (open) state, the structure surprisingly did not feature many functionally important interactions established by previous biochemical and electrophysiology experiments. Using Molecular Dynamics Flexible Fitting (MDFF), we refined the structure and recovered the missing functionally relevant salt bridges in hERG in its depolarized state. We also performed electrophysiology experiments to confirm the functional relevance of a novel salt bridge predicted by our refinement protocol. Our work shows how refinement of a high-resolution cryo-EM structure helps to bridge the existing gap between the structure and function in the voltage-sensing domain (VSD) of hERG.Statement of SignificanceCryo-EM has emerged as a major breakthrough technique in structural biology of membrane proteins. However, even high-resolution Cryo-EM structures contain poor side chain conformations and interatomic clashes. A high-resolution cryo-EM structure of hERG1 has been solved in the depolarized (open) state. The state captured by Cryo-EM surprisingly did not feature many functionally important interactions established by previous experiments. Molecular Dynamics Flexible Fitting (MDFF) used to enable refinement of the hERG1 channel structure in complex membrane environment re-establishing key functional interactions in the voltage sensing domain.

scholarly journals Probing Ion Channel Structure and Function Using Light-Sensitive Amino Acids

2018 ◽  
Vol 43 (6) ◽  
pp. 436-451 ◽  
Author(s):  
Viktoria Klippenstein ◽  
Laetitia Mony ◽  
Pierre Paoletti
Keyword(s):  
Amino Acids ◽  
Ion Channel ◽  
Structure And Function ◽  
Channel Structure ◽  
And Function
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