2K44

Solution structure of a K+-channel voltage-sensor paddle domain

2K44 の概要

• エントリーDOI: 10.2210/pdb2k44/pdb
• 分子名称: K+-channel voltage-sensor paddle domain of Calcium-activated potassium channel subunit alpha-1 (1 entity in total)
• 機能のキーワード: potassium channel, voltage-sensor, membrane, micelle, solution structure, membrane protein
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q12791
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3385.02

構造登録者

Unnerstale, S.,Lind, J.,Papadopoulos, E.,Maler, L. (登録日: 2008-05-28, 公開日: 2009-06-02, 最終更新日: 2024-05-29)

主引用文献

Unnerstale, S.,Lind, J.,Papadopoulos, E.,Maler, L.
Solution structure of the HsapBK K+-channel voltage-sensor paddle sequence
Biochemistry, 2009

PubMed Abstract: Voltage-gated potassium channels open and close in response to changes in the membrane potential. In this study, we have determined the NMR solution structure of the putative S3b-S4 voltage-sensor paddle fragment, the part that moves to mediate voltage gating, of the HsapBK potassium channel in dodecylphosphocholine (DPC) micelles. This paper presents the first structure of the S3b-S4 fragment from a BK channel. Diffusion coefficients as determined from PFG NMR experiments showed that a well-defined complex between the peptide and DPC molecules was formed. The structure reveals a helix-turn-helix motif, which is in agreement with crystal structures of other voltage-gated potassium channels, thus indicating that it is feasible to study the isolated fragment. The paddle motifs generally contain several basic residues, implicated in the gating. The critical Arg residues in this structure all reside on the surface, which is in agreement with crystal structures of K(v) channels. Similarities in the structure of the S3b-S4 fragment in BK and K(v) channels as well as important differences are seen, which may be important for explaining the details in paddle movement within a bilayer.

PubMed: 19456106
DOI: 10.1021/bi9004599

実験手法

SOLUTION NMR