ArticleBiophysical journal2008
Energetics of divalent selectivity in a calcium channel: the ryanodine receptor case study.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 167 citations in OpenAlex.
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- Ryanodine Receptor Open Times Are Determined in the Closed State.Biophysical journal · 2018Article
- Conic shapes have higher sensitivity than cylindrical ones in nanopore DNA sequencing.Scientific reports · 2018Article
- In silico assessment of the conduction mechanism of the Ryanodine Receptor 1 reveals previously unknown exit pathways.Scientific reports · 2018Article
- Sarcoplasmic Reticulum CaBiophysical journal · 2018Article
- The structural basis of ryanodine receptor ion channel function.The Journal of general physiology · 2017Review
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1 author at 1 institution in 1 country.
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Abstract
A model of the ryanodine receptor (RyR) calcium channel is used to study the energetics of binding selectivity of Ca(2+) versus monovalent cations. RyR is a calcium-selective channel with a DDDD locus in the selectivity filter, similar to the EEEE locus of the L-type calcium channel. While the affinity of RyR for Ca(2+) is in the millimolar range (as opposed to the micromolar range of the L-type channel), the ease of single-channel measurements compared to L-type and its similar selectivity filter make RyR an excellent candidate for studying calcium selectivity. A Poisson-Nernst-Planck/density functional theory model of RyR is used to calculate the energetics of selectivity. Ca(2+) versus monovalent selectivity is driven by the charge/space competition mechanism in which selectivity arises from a balance of electrostatics and the excluded volume of ions in the crowded selectivity filter. While electrostatic terms dominate the selectivity, the much smaller excluded-volume term also plays a substantial role. In the D4899N and D4938N mutations of RyR that are analyzed, substantial changes in specific components of the chemical potential profiles are found far from the mutation site. These changes result in the significant reduction of Ca(2+) selectivity found in both theory and experiments.
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