1T1D

CRYSTAL STRUCTURE OF THE TETRAMERIZATION DOMAIN OF THE SHAKER POTASSIUM CHANNEL

1T1D の概要

• エントリーDOI: 10.2210/pdb1t1d/pdb
• 分子名称: PROTEIN (POTASSIUM CHANNEL KV1.1) (2 entities in total)
• 機能のキーワード: potassium channels, tetramerization domain, 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: 12097.45

構造登録者

Kreusch, A.,Pfaffinger, P.J.,Stevens, C.F.,Choe, S. (登録日: 1998-09-22, 公開日: 1999-01-13, 最終更新日: 2023-08-23)

主引用文献

Bixby, K.A.,Nanao, M.H.,Shen, N.V.,Kreusch, A.,Bellamy, H.,Pfaffinger, P.J.,Choe, S.
Zn2+-binding and molecular determinants of tetramerization in voltage-gated K+ channels.
Nat.Struct.Biol., 6:38-43, 1999

PubMed Abstract: The N-terminal, cytoplasmic tetramerization domain (T1) of voltage-gated K+ channels encodes molecular determinants for subfamily-specific assembly of alpha-subunits into functional tetrameric channels. Crystal structures of T1 tetramers from Shaw and Shaker subfamilies reveal a common four-layered scaffolding. Within layer 4, on the hypothetical membrane-facing side of the tetramer, the Shaw T1 tetramer contains four zinc ions; each is coordinated by a histidine and two cysteines from one monomer and by one cysteine from an adjacent monomer. The amino acids involved in coordinating the Zn2+ ion occur in a HX5CX20CC sequence motif that is highly conserved among all Shab, Shaw and Shal subfamily members, but is not found in Shaker subfamily members. We demonstrate by coimmunoprecipitation that a few characteristic residues in the subunit interface are crucial for subfamily-specific tetramerization of the T1 domains.

PubMed: 9886290
DOI: 10.1038/4911

実験手法

X-RAY DIFFRACTION (1.51 Å)