ArticleStructure (London, England : 1993)2014
State-dependent network connectivity determines gating in a K+ channel.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Dietary anions control potassium excretion: it is more than a poorly absorbable anion effect.American journal of physiology. Renal physiology · 2023Article
- LRET Determination of Molecular Distances during pH Gating of the Mammalian Inward Rectifier Kir1.1b.Biophysical journal · 2018Article
- Structural dynamics of potassium-channel gating revealed by single-molecule FRET.Nature structural & molecular biology · 2016Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- Article
- Insights into the structural nature of the transition state in the Kir channel gating pathway.Channels (Austin, Tex.) · 2014Article
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Authors and funding
7 authors.
Funding
Abstract
X-ray crystallography has provided tremendous insight into the different structural states of membrane proteins and, in particular, of ion channels. However, the molecular forces that determine the thermodynamic stability of a particular state are poorly understood. Here we analyze the different X-ray structures of an inwardly rectifying potassium channel (Kir1.1) in relation to functional data we obtained for over 190 mutants in Kir1.1. This mutagenic perturbation analysis uncovered an extensive, state-dependent network of physically interacting residues that stabilizes the pre-open and open states of the channel, but fragments upon channel closure. We demonstrate that this gating network is an important structural determinant of the thermodynamic stability of these different gating states and determines the impact of individual mutations on channel function. These results have important implications for our understanding of not only K+ channel gating but also the more general nature of conformational transitions that occur in other allosteric proteins.
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