Key result
Covalent modification of Kir2.1 channels reveals the inner pore binds three Mg2+ ions simultaneously.
The inner pore of Kir2.1 channels is unprecedentedly wide, facilitating ion permeation and high-affinity binding of multiple pore blockers to generate strong inward rectification.
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Kir2.1 pore architecture may guide blocker design; extends channel models but leaves open human cardiac relevance.
Lü et al. (1999) studied this question. Covalent attachment of positively charged moieties to Kir2.1 channels was evaluated on Architecture of the inner pore and subconductance levels. Covalent modification of Kir2.1 channels revealed that the inner pore is formed solely by the second transmembrane segment and is wide enough to bind three Mg2+ ions or polyamines simultaneously.
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