Batista C V, Gómez-Lagunas F, Lucas S, Possani L D
Department of Molecular Recognition and Structural Biology, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Mexico.
FEBS Lett. 2000 Dec 8;486(2):117-20. doi: 10.1016/s0014-5793(00)02253-5.
A new peptide, Tc1, containing only 23 amino acids closely packed by three disulfide bridges was isolated from the Amazonian scorpion Tityus cambridgei. It blocks reversibly the Shaker B K(+)-channels with a K(d) of 65 nM and displaces binding of noxiustoxin to mouse brain synaptosome membranes. It is the shortest known peptide from scorpion venom that recognizes K(+)-channels and constitutes a new structural subfamily of toxin, classified as alphaKTx 13.1.
一种仅含23个氨基酸且由三个二硫键紧密排列的新肽Tc1，是从亚马逊蝎子剑桥蒂氏蝎中分离出来的。它能以65 nM的解离常数可逆性阻断Shaker B钾通道，并取代诺蝎毒素与小鼠脑突触体膜的结合。它是已知最短的能识别钾通道的蝎毒肽，构成了一个新的毒素结构亚家族，被归类为αKTx 13.1。
