The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel.

Minor DL, Lin YF, Mobley BC, Avelar A, Jan YN, Jan LY, Berger JM
Cell. 2000 102 (5): 657-70

PMID: 11007484 · DOI:10.1016/s0092-8674(00)00088-x

Kv voltage-gated potassium channels share a cytoplasmic assembly domain, T1. Recent mutagenesis of two T1 C-terminal loop residues implicates T1 in channel gating. However, structural alterations of these mutants leave open the question concerning direct involvement of T1 in gating. We find in mammalian Kv1.2 that gating depends critically on residues at complementary T1 surfaces in an unusually polar interface. An isosteric mutation in this interface causes surprisingly little structural alteration while stabilizing the closed channel and increasing the stability of T1 tetramers. Replacing T1 with a tetrameric coiled-coil destabilizes the closed channel. Together, these data suggest that structural changes involving the buried polar T1 surfaces play a key role in the conformational changes leading to channel opening.

MeSH Terms (19)

Amino Acid Substitution Animals Binding Sites Circular Dichroism Crystallography, X-Ray Electrophysiology Ion Channel Gating Kv1.2 Potassium Channel Models, Molecular Mutation Oocytes Potassium Potassium Channels Potassium Channels, Voltage-Gated Protein Structure, Secondary Protein Structure, Tertiary Static Electricity Structure-Activity Relationship Xenopus laevis

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