Garcia-Valdes J, Zamudio F Z, Toro L, Possani L D
Department of Molecular Recognition and Structural Biology, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Mexico.
FEBS Lett. 2001 Sep 21;505(3):369-73. doi: 10.1016/s0014-5793(01)02791-0.
A novel peptide from Centruroides noxius Hoffmann scorpion venom was isolated and sequenced. The 37 amino acid peptide belongs to the charybdotoxin sub-family (alphaKTx1) and was numbered member 11. alphaKTx1.11 has 75% sequence identity with iberiotoxin and 54% with charybdotoxin. alphaKTx1.11 revealed specificity for mammalian MaxiK channels (hSlo), thus, was named slotoxin. Slotoxin blocks the MaxiK pore-forming alpha subunit reversibly (K(d)=1.5 nM). Slotoxin association with alpha+beta (beta1 or beta4) channels was approximately 10 times slower than iberiotoxin and charybdotoxin, leading to a lack of effect on alpha+beta4 when tested at 100 nM for 5 min. Thus, slotoxin is a better tool to distinguish MaxiK alpha+beta complexes.
从墨西哥毒蝎(Centruroides noxius Hoffmann)毒液中分离并测序出一种新型肽。这种由37个氨基酸组成的肽属于卡律布狄斯毒素亚家族(alphaKTx1),被编号为成员11,即alphaKTx1.11。alphaKTx1.11与iberiotoxin的序列同一性为75%,与卡律布狄斯毒素的序列同一性为54%。alphaKTx1.11对哺乳动物大电导钙激活钾通道(hSlo)具有特异性,因此被命名为slotoxin。Slotoxin可逆地阻断大电导钙激活钾通道的孔形成α亚基(K(d)=1.5 nM)。Slotoxin与α+β(β1或β4)通道的结合速度比iberiotoxin和卡律布狄斯毒素慢约10倍,在100 nM下测试5分钟时,对α+β4没有影响。因此,slotoxin是区分大电导钙激活钾通道α+β复合物的更好工具。