Production of recombinant Conkunitzin-S1 in Escherichia coli
Production of recombinant Conkunitzin-S1 in Escherichia coli
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DOI：
10.1016/j.pep.2006.01.019
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发表时间：
2006-06-01
影响因子：
1.6
通讯作者：
Becker, Stefan
中科院分区：
文献类型：
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作者：
Bayrhuber, Monika;Graf, Roland;Becker, Stefan
Conkunitzin-S1来自圆锥螺Conus striatus，是具有典型Kunitz结构域折叠的新神经毒素家族的第一成员。Conk-SI是60个氨基酸长，并且缺乏通常在Kunitz结构域模块中发现的三个保守二硫键之一。其特异性结合至Shaker家族的电压激活钾通道。该肽以与N-末端内含肽融合的不溶性形式表达。在谷胱甘肽的存在下再折叠，然后通过pH变化诱导的融合蛋白的裂解导致在一个功能性毒素，如通过电压钳测量所示。(c)2006年爱思唯尔公司All rights reserved.
Conkunitzin-S1 from the cone snail Conus striatus is the first member of a new neurotoxin family with a canonical Kunitz domain fold. Conk-SI is 60 amino acids long and lacks one of the three conserved disulfide bonds typically found in Kunitz domain modules. It binds specifically to voltage activated potassium channels of the Shaker family. The peptide was expressed in insoluble form in fusion with an N-terminal intein. Refolding in the presence of glutathione followed by pH shift-induced cleavage of the fusion protein resulted in a functional toxin as demonstrated by voltage-clamp measurements. (c) 2006 Elsevier Inc. All rights reserved.