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Characterization of the outer pore region of the apamin-sensitive Ca2+-activated K+ channel rSK2.蜂毒明肽敏感的Ca2+激活K+通道rSK2外孔区域的特性分析
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Rapid and efficient site-specific mutagenesis without phenotypic selection.无需表型筛选的快速高效位点特异性诱变。
Proc Natl Acad Sci U S A. 1985 Jan;82(2):488-92. doi: 10.1073/pnas.82.2.488.
2
Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain.哺乳动物大脑中电压门控钾通道功能多样性的分子基础。
EMBO J. 1989 Nov;8(11):3235-44. doi: 10.1002/j.1460-2075.1989.tb08483.x.
3
Competition for block of a Ca2(+)-activated K+ channel by charybdotoxin and tetraethylammonium.由沙蚕毒素和四乙铵对钙激活钾通道的阻断竞争
Neuron. 1988 Dec;1(10):1003-6. doi: 10.1016/0896-6273(88)90157-2.
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Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel.大电导钙激活钾通道的蝎毒素阻断机制
J Gen Physiol. 1988 Mar;91(3):335-49. doi: 10.1085/jgp.91.3.335.
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Sequence of a probable potassium channel component encoded at Shaker locus of Drosophila.果蝇振颤基因座编码的一种可能的钾通道成分的序列。
Science. 1987 Aug 14;237(4816):770-5. doi: 10.1126/science.2441471.
6
Mutations affecting TEA blockade and ion permeation in voltage-activated K+ channels.影响电压激活钾通道中TEA阻断和离子通透的突变。
Science. 1990 Oct 12;250(4978):276-9. doi: 10.1126/science.2218530.
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Functional characterization of a minimal K+ channel expressed from a synthetic gene.一个由合成基因表达的最小钾离子通道的功能特性
Biochemistry. 1991 Apr 2;30(13):3341-6. doi: 10.1021/bi00227a025.
8
Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels.钾通道肽阻断剂刺尾鱼毒素基因的设计、合成及功能表达
Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2046-50. doi: 10.1073/pnas.88.6.2046.
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Three-dimensional structure of natural charybdotoxin in aqueous solution by 1H-NMR. Charybdotoxin possesses a structural motif found in other scorpion toxins.
Eur J Biochem. 1991 Feb 26;196(1):19-28. doi: 10.1111/j.1432-1033.1991.tb15780.x.
10
Mapping the receptor site for charybdotoxin, a pore-blocking potassium channel inhibitor.绘制孔道阻断型钾通道抑制剂加勒比海毒素的受体位点图谱。
Neuron. 1990 Dec;5(6):767-71. doi: 10.1016/0896-6273(90)90335-d.

A point mutation in a Shaker K+ channel changes its charybdotoxin binding site from low to high affinity.

作者信息

Goldstein S A, Miller C

机构信息

Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110.

出版信息

Biophys J. 1992 Apr;62(1):5-7. doi: 10.1016/S0006-3495(92)81760-5.

DOI:10.1016/S0006-3495(92)81760-5
PMID:1376173
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1260466/
Abstract
摘要