1TSK
SCORPION TOXIN (TS KAPPA) FROM TITYUS SERRULATUS ACTIVE ON SMALL CONDUCTANCE POTASSIUM CHANNEL, NMR, 30 STRUCTURES
1TSK の概要
| エントリーDOI | 10.2210/pdb1tsk/pdb |
| 分子名称 | TS KAPA (1 entity in total) |
| 機能のキーワード | scorpion, toxin, tityus serrulatus, potassium channel, ts kapa, neurotoxin |
| 由来する生物種 | Tityus serrulatus (Brazilian scorpion) |
| 細胞内の位置 | Secreted: P56219 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 3791.48 |
| 構造登録者 | |
| 主引用文献 | Blanc, E.,Lecomte, C.,Rietschoten, J.V.,Sabatier, J.M.,Darbon, H. Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca(2+)-activated K+ channels. Proteins, 29:359-369, 1997 Cited by PubMed Abstract: TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apamin-sensitive calcium-activated potassium channels (SK). It is able to efficiently compete with apamin for binding on this channel (K0.5 = 0.3 nM) [Legros, C. et al., FEBS Lett. 390:81-84, 1996]. The solution structure of TsK has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a short alpha helix from residues 14 to 20 and a three-stranded antiparallel beta sheet (residues 2-3, 27-29, and 32-34). The interaction of TsK with the SK potassium channel has been modeled according to the charge anisotropy of the ligand. The resulting dipole moment orientates TsK so that it presents toward the receptor, a surface, mainly basic, encompassing residues K18 and K19 on one side and R9 and Y8 on the other. Despite its three-dimensional structure that is related with scorpion toxins active on voltage-gated potassium channels such as charybdotoxin, the pharmacological activity and specificity of TsK is related with shorter scorpion toxins (i.e., possessing an only two-stranded beta sheet) such as scyllatoxin (also named leiurotoxin I) or P05. PubMed: 9365990DOI: 10.1002/(SICI)1097-0134(199711)29:3<359::AID-PROT9>3.3.CO;2-V 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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