F-肌动蛋白的鬼笔环肽结合位点。
The phalloidin binding site of F-actin.
作者信息
Vandekerckhove J, Deboben A, Nassal M, Wieland T
出版信息
EMBO J. 1985 Nov;4(11):2815-8. doi: 10.1002/j.1460-2075.1985.tb04008.x.
Abstract
Tritium-containing affinity-labelling derivatives of phalloidin, an alkylating iodoacetyl compound (EAL) and a photolabile, carbene generating diazirine (PAL), have been reacted with rabbit muscle actin, the former after protection of thiol groups with N-ethylmaleimide. Labelled peptides generated by tryptic and/or thermolysin digestion were isolated by paper peptide mapping and characterized by determination of their amino acid sequences. EAL binds to methionine-119 and methionine-355; PAL binds to glutamic acid-117. These residues are located in regions with extremely conserved amino acid sequences. The cleft between the two domains of the actin monomer is suggested as the possible binding site for phalloidin.
摘要
用含有氚的鬼笔环肽亲和标记衍生物、一种烷基化碘乙酰化合物（EAL）和一种光不稳定的、能产生卡宾的重氮丙啶（PAL）与兔肌肉肌动蛋白反应，前者在用N - 乙基马来酰亚胺保护巯基后进行反应。通过纸层析肽图谱分离经胰蛋白酶和/或嗜热菌蛋白酶消化产生的标记肽，并通过测定其氨基酸序列进行表征。EAL与甲硫氨酸 - 119和甲硫氨酸 - 355结合；PAL与谷氨酸 - 117结合。这些残基位于氨基酸序列极其保守的区域。肌动蛋白单体两个结构域之间的裂隙被认为是鬼笔环肽可能的结合位点。
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