1DSX

KV1.2 T1 DOMAIN, RESIDUES 33-119, T46V MUTANT

1DSX の概要

• エントリーDOI: 10.2210/pdb1dsx/pdb
• 分子名称: PROTEIN (KV1.2 VOLTAGE-GATED POTASSIUM CHANNEL) (2 entities in total)
• 機能のキーワード: voltage-gated potassium channel, assembly domain, tetramer, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P63142
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 83967.93

構造登録者

Minor Jr., D.L.,Lin, Y.-F.,Mobley, B.C.,Avelar, A.,Jan, Y.N.,Jan, L.Y.,Berger, J.M. (登録日: 2000-01-10, 公開日: 2000-09-20, 最終更新日: 2024-02-07)

主引用文献

Minor, D.L.,Lin, Y.F.,Mobley, B.C.,Avelar, A.,Jan, Y.N.,Jan, L.Y.,Berger, J.M.
The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel.
Cell(Cambridge,Mass.), 102:657-670, 2000

PubMed Abstract: 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.

PubMed: 11007484
DOI: 10.1016/S0092-8674(00)00088-X

実験手法

X-RAY DIFFRACTION (1.6 Å)