Key result
Mutations in the GYGD motif of the rat drk1 K+ channel revealed a co-operative intersubunit interaction between the tyrosine and aspartate positions that determines ion selectivity and gating.
Population
Rat drk1 (Kv2.1) K+ channel and bacterial KcsA K+ channel models
Design
Preclinical
Authors
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Informs K+ channel selectivity mechanisms in rats; leaves open translation to human cardiac electrophysiology.
The study reveals that the aspartate (D) position in the GYGD motif of K+ channels fine-tunes ion selectivity through functional interaction with the tyrosine (Y) position in neighboring subunits.
Chapman et al. (2001) studied this question. Mutations of the GYGD motif in the rat drk1 (Kv2.1) K+ channel was evaluated on Ion selectivity, single channel conductance, and open state stability. Mutations in the GYGD motif of the rat drk1 K+ channel revealed a co-operative intersubunit interaction between the tyrosine and aspartate positions that determines ion selectivity and gating.
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