ArticleThe Journal of biological chemistry2011
Interactions of cations with the cytoplasmic pores of inward rectifier K(+) channels in the closed state.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019Article
- Functional mapping of the N-terminal arginine cluster and C-terminal acidic residues of Kir6.2 channel fused to a G protein-coupled receptor.Biochimica et biophysica acta. Biomembranes · 2017Article
- Structure of a highly acidic β-lactamase from the moderate halophile Chromohalobacter sp. 560 and the discovery of a Cs(+)-selective binding site.Acta crystallographica. Section D, Biological crystallography · 2015Article
- The bundle crossing region is responsible for the inwardly rectifying internal spermine block of the Kir2.1 channel.Pflugers Archiv : European journal of physiology · 2014Article
- Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.The Journal of biological chemistry · 2014Article
- Conformational changes underlying pore dilation in the cytoplasmic domain of mammalian inward rectifier K+ channels.PloS one · 2013Article
- Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation.Structure (London, England : 1993) · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ion channels gate at membrane-embedded domains by changing their conformation along the ion conduction pathway. Inward rectifier K(+) (Kir) channels possess a unique extramembrane cytoplasmic domain that extends this pathway. However, the relevance and contribution of this domain to ion permeation remain unclear. By qualitative x-ray crystallographic analysis, we found that the pore in the cytoplasmic domain of Kir3.2 binds cations in a valency-dependent manner and does not allow the displacement of Mg(2+) by monovalent cations or spermine. Electrophysiological analyses revealed that the cytoplasmic pore of Kir3.2 selectively binds positively charged molecules and has a higher affinity for Mg(2+) when it has a low probability of being open. The selective blocking of chemical modification of the side chain of pore-facing residues by Mg(2+) indicates that the mode of binding of Mg(2+) is likely to be similar to that observed in the crystal structure. These results indicate that the Kir3.2 crystal structure has a closed conformation with a negative electrostatic field potential at the cytoplasmic pore, the potential of which may be controlled by conformational changes in the cytoplasmic domain to regulate ion diffusion along the pore.
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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.