ArticleStructure (London, England : 1993)2012
Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The allosteric gating mechanism of the MthK channel.National science review · 2022Article
- Article
- Polyamine blockade and binding energetics in the MthK potassium channel.The Journal of general physiology · 2020Article
- Activation of a nucleotide-dependent RCK domain requires binding of a cation cofactor to a conserved site.eLife · 2019Article
- Article
- Permeating disciplines: Overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport.Biochimica et biophysica acta. Biomembranes · 2018Review
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Initial steps of inactivation at the K+ channel selectivity filter.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
4 authors.
Funding
Abstract
RCK domains control activity of a variety of K(+) channels and transporters through binding of cytoplasmic ligands. To gain insight toward mechanisms of RCK domain activation, we solved the structure of the RCK domain from the Ca(2+)-gated K(+) channel, MthK, bound with Ba(2+), at 3.1 Å resolution. The Ba(2+)-bound RCK domain was assembled as an octameric gating ring, as observed in structures of the full-length MthK channel, and shows Ba(2+) bound at several positions. One of the Ba(2+) sites, termed C1, overlaps with a known Ca(2+)-activation site, determined by residues D184 and E210. Functionally, Ba(2+) can activate reconstituted MthK channels as observed in electrophysiological recordings, whereas Mg(2+) (up to 100 mM) was ineffective. Ba(2+) activation was abolished by the mutation D184N, suggesting that Ba(2+) activates primarily through the C1 site. Our results suggest a working hypothesis for a sequence of ligand-dependent conformational changes that may underlie RCK domain activation and channel gating.
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