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- W2017483500 abstract "Inward rectifiers are a subfamily of potassium channels that control the amounts of outward K+ current in a cell. These channels achieve rectification through intracellular block by strongly charged cations such as Mg2+ and polyamines like spermine (SPM4+). The large cytoplasmic domain that extends the ion permeation pathway has been shown to be an important determinant of conductance and rectification, however the organization of ions within this part of the pore is not well understood. In this study, the properties of ions inside the cytoplasmic domains of a weak (Kir1.1/ROMK) and strong (Kir2.1/IRK) rectifier are investigated via explicit solvent molecular dynamics simulations in 1M KCl. Both channels concentrate K+ ions in large amounts (local concentration > 3M), with the highest densities near the protein surface. An additional concentrating region specific to Kir2.1/IRK is observed near the cytoplasmic opening. Simulations are also carried out with Mg2+ or SPM4+ inside the domain. Mg2+ interacts directly with pore-lining residues, resulting in a depletion of K+ and increase in the local concentration of Cl−. SPM4+ shows high density throughout the central pore and selectively depletes K+ in the upper region of the pore closest to the transmembrane domain. Two long-lived states of SPM4+ are observed in Kir2.1/IRK: (i) inside the central pore in contact with residues D2591, E2241, E2242 and E2992 from two adjacent subunits, and (ii) near the cytoplasmic entrance interacting with residues D255, D259 and E224 on a single monomer. These results demonstrate a level of molecular specificity with respect to ion behavior within the cytoplasmic domains that could correspond to differences in rectification properties." @default.
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- W2017483500 date "2009-02-01" @default.
- W2017483500 modified "2023-10-16" @default.
- W2017483500 title "The Behavior of Ions Inside the Cytoplasmic Domain of Inward Rectifier Potassium Channels" @default.
- W2017483500 doi "https://doi.org/10.1016/j.bpj.2008.12.2383" @default.
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