ENGINEERING A UNIQUELY REACTIVE THIOL INTO A CYSTEINE-RICH PEPTIDE

被引:23
作者
SHIMONY, E
SUN, TY
KOLMAKOVAPARTENSKY, L
MILLER, C
机构
[1] Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, MA
来源
PROTEIN ENGINEERING | 1994年 / 7卷 / 04期
关键词
CHARYBDOTOXIN; LABELING; POTASSIUM CHANNEL;
D O I
10.1093/protein/7.4.503
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cysteine mutagenesis for the purpose of chemical labelling was applied to the K+ channel neurotoxin charybdotoxin, a 37-residue peptide with six functionally essential cysteines. An additional 'spinster cysteine' was introduced at a position far away in space from the toxin's known interaction surface where it contacts its K+ channel receptor. Despite the presence of the extra unpaired cysteine residue, the toxin still folds efficiently and may be labelled by fluorescent and radioactive reagents to give a functionally competent toxin.
引用
收藏
页码:503 / 507
页数:5
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