1KKD

Solution structure of the calmodulin binding domain (CaMBD) of small conductance Ca2+-activated potassium channels (SK2)

1KKD の概要

• エントリーDOI: 10.2210/pdb1kkd/pdb
• 関連するPDBエントリー: 1G4Y
• 分子名称: Small conductance calcium-activated potassium channel protein 2 (1 entity in total)
• 機能のキーワード: small-conductance calcium-activated potassium channel, calmodulin binding domain (cambd), channel gating, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P70604
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12243.40

構造登録者

Wissmann, R.,Bildl, W.,Neumann, H.,Rivard, A.F.,Kloecker, N.,Weitz, D.,Schulte, U.,Adelman, J.P.,Bentrop, D.,Fakler, B. (登録日: 2001-12-07, 公開日: 2001-12-14, 最終更新日: 2024-05-22)

主引用文献

Wissmann, R.,Bildl, W.,Neumann, H.,Rivard, A.F.,Klocker, N.,Weitz, D.,Schulte, U.,Adelman, J.P.,Bentrop, D.,Fakler, B.
A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin.
J.Biol.Chem., 277:4558-4564, 2002

PubMed Abstract: Small conductance Ca(2+)-activated potassium (SK) channels underlie the afterhyperpolarization that follows the action potential in many types of central neurons. SK channels are voltage-independent and gated solely by intracellular Ca(2+) in the submicromolar range. This high affinity for Ca(2+) results from Ca(2+)-independent association of the SK alpha-subunit with calmodulin (CaM), a property unique among the large family of potassium channels. Here we report the solution structure of the calmodulin binding domain (CaMBD, residues 396-487 in rat SK2) of SK channels using NMR spectroscopy. The CaMBD exhibits a helical region between residues 423-437, whereas the rest of the molecule lacks stable overall folding. Disruption of the helical domain abolishes constitutive association of CaMBD with Ca(2+)-free CaM, and results in SK channels that are no longer gated by Ca(2+). The results show that the Ca(2+)-independent CaM-CaMBD interaction, which is crucial for channel function, is at least in part determined by a region different in sequence and structure from other CaM-interacting proteins.

PubMed: 11723128
DOI: 10.1074/jbc.M109240200

実験手法

SOLUTION NMR