ArticleBiochemistry2014
Conformational dynamics at the inner gate of KcsA during activation.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination.Journal of molecular biology · 2018Article
- Expression and Purification of the Pain Receptor TRPV1 for Spectroscopic Analysis.Scientific reports · 2017Article
- Probing Conformational Changes during the Gating Cycle of a Potassium Channel in Lipid Bilayers.Biophysical journal · 2017Article
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- Allosteric coupling between proximal C-terminus and selectivity filter is facilitated by the movement of transmembrane segment 4 in TREK-2 channel.Scientific reports · 2016Article
- Conformational Response of Influenza A M2 Transmembrane Domain to Amantadine Drug Binding at Low pH (pH 5.5).Frontiers in physiology · 2016Article
- Ion-binding properties of a K+ channel selectivity filter in different conformations.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- An Integrated Framework Advancing Membrane Protein Modeling and Design.PLoS computational biology · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The potassium channel KcsA offers a unique opportunity to explicitly study the dynamics of the moving parts of ion channels, yet our understanding of the extent and dynamic behavior of the physiologically relevant structural changes at the inner gate in KcsA remains incomplete. Here, we use electron paramagnetic resonance, nuclear magnetic resonance, and molecular dynamics simulations to characterize the extent of pH-dependent conformational changes of the inner gate in lipid bilayers or detergent micelles. Our results show that under physiological conditions the inner gate experiences a maximal diagonal opening of ∼24 Å with the largest degree of dynamics near the pKa of activation (pH ∼3.9). These results extend the observation that the C-terminus is necessary to limit the extent of opening and imply that the inner gate regulates the extent of conformational change at the zone of allosteric coupling and at the selectivity filter.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.