1BYW

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL

1BYW の概要

• エントリーDOI: 10.2210/pdb1byw/pdb
• 分子名称: PROTEIN (HUMAN ERG POTASSIUM CHANNEL) (2 entities in total)
• 機能のキーワード: pas domain, potassium channel domain, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane ; Multi- pass membrane protein : Q12809
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12346.40

構造登録者

Cabral, J.H.M.,Lee, A.,Mackinnon, R. (登録日: 1998-10-15, 公開日: 1998-12-16, 最終更新日: 2024-02-07)

主引用文献

Cabral, J.H.M.,Lee, A.,Cohen, S.L.,Chait, B.T.,Li, M.,Mackinnon, R.
Crystal Structure and Functional Analysis of the Herg Potassium Channel N-Terminus: A Eukaryotic Pas Domain
Cell(Cambridge,Mass.), 95:649-655, 1998

PubMed Abstract: The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function.

PubMed: 9845367
DOI: 10.1016/S0092-8674(00)81635-9

実験手法

X-RAY DIFFRACTION (2.6 Å)