1EOD

CRYSTAL STRUCTURE OF THE N136D MUTANT OF A SHAKER T1 DOMAIN

1EOD の概要

• エントリーDOI: 10.2210/pdb1eod/pdb
• 関連するPDBエントリー: 1EOE 1EOF 1T1D
• 分子名称: POTASSIUM CHANNEL KV1.1 (2 entities in total)
• 機能のキーワード: potassium channels, aplysia kv1.1, proton transport, membrane protein
• 由来する生物種: Aplysia californica (California sea hare)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12098.44

構造登録者

Nanao, M.H.,Cushman, S.J.,Jahng, A.W.,DeRubeis, D.,Choe, S.,Pfaffinger, P.J. (登録日: 2000-03-22, 公開日: 2000-05-02, 最終更新日: 2024-02-07)

主引用文献

Cushman, S.J.,Nanao, M.H.,Jahng, A.W.,DeRubeis, D.,Choe, S.,Pfaffinger, P.J.
Voltage dependent activation of potassium channels is coupled to T1 domain structure.
Nat.Struct.Biol., 7:403-407, 2000

PubMed Abstract: The T1 domain, a highly conserved cytoplasmic portion at the N-terminus of the voltage-dependent K+ channel (Kv) alpha-subunit, is responsible for driving and regulating the tetramerization of the alpha-subunits. Here we report the identification of a set of mutations in the T1 domain that alter the gating properties of the Kv channel. Two mutants produce a leftward shift in the activation curve and slow the channel closing rate while a third mutation produces a rightward shift in the activation curve and speeds the channel closing rate. We have determined the crystal structures of T1 domains containing these mutations. Both of the leftward shifting mutants produce similar conformational changes in the putative membrane facing surface of the T1 domain. These results suggest that the structure of the T1 domain in this region is tightly coupled to the channel's gating states.

PubMed: 10802739
DOI: 10.1038/75185

実験手法

X-RAY DIFFRACTION (2.45 Å)