Site directed mutants of Noxiustoxin reveal specific interactions with potassium channels

被引：19

作者：

Martínez, F

Muñoz-Garay, C

Gurrola, G

Darszon, A

Possani, LD

Becerril, B

机构：

[1] Univ Nacl Autonoma Mexico, Dept Mol Recognit & Struct Biol, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico

[2] Univ Nacl Autonoma Mexico, Dept Genet & Mol Physiol, Inst Biotecnol, Cuernavaca 62210, Morelos, Mexico

来源：

FEBS LETTERS | 1998年 / 429卷 / 03期

关键词：

Centruroides noxius; K+ channel; mutagenesis; oocyte expression; noxiustoxin; scorpion toxin;

D O I：

10.1016/S0014-5793(98)00636-X

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：

Several site directed mutations mere introduced into a synthetic Noxiustoxin (NTX) gene. Alanine scanning of the nonapeptide at the N-terminal segment of NTX (threonine 1 (T1) to serine 9 (S9)) was constructed and the recombinant products were obtained in pure form. Additionally, lysine 28 (K28) was changed to arginine (R) or glutamic acid (E), cysteine 29 was changed to alanine, and residues 37-39 (TSr-Asn-Asn) of the carboxyl end were deleted. The recombinant mutants mere tested for their ability to displace I-125-NTX from rat brain synaptosome membranes, as well as for their efficiency in blocking the activity of K(v)1.1 K+ channels expressed in Xenopus laevis oocytes. The main results indicate that residues K6, T8 at the amino end, and K28 and the tripeptide YNN at the carboxyl end are involved in specific interactions of NTX with rat brain and/or K(v)1.1 K+ channels. (C) 1998 Federation of European Biochemical Societies.

引用

页码：381 / 384

页数：4

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