Comparative pharmacology and cloning of two novel arachnid sodium channels: Exploring the adaptive insensitivity of scorpion to its toxins
文献类型:期刊论文
作者 | Zuo, XP ; He, HQ ; He, M ; Liu, ZR ; Xu, Q ; Ye, JG ; Ji, YH |
刊名 | FEBS LETTERS
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出版日期 | 2006 |
卷号 | 580期号:18页码:4508 |
关键词 | BUTHUS-MARTENSI KARSCH GATED NA+ CHANNELS BETA-TOXINS FUNCTIONAL SURFACE RECEPTOR-SITES INSECT VENOM BMK NEUROTOXINS BINDING |
ISSN号 | 0014-5793 |
通讯作者 | Ji, YH: Shanghai Univ, Sch Life Sci, Shang Da Rd 99, Shanghai 200444, Peoples R China. |
中文摘要 | Scorpion toxins have been found lacking effect on Na+ current of its own sodium channel, whereas the molecular mechanism remains mystery. In this study, the binding affinity of pharmacologically distinct scorpion toxins was found much weaker to scorpion (Buthus martensii) nerve synaptosomes than to spider (Ornithoctonus huwena) ones. The sodium channel cDNA from these two species were further cloned. The deduced proteins contain 1871 and 1987 amino acids respectively. Several key amino acid substitutions, i.e., A161OV, 11611L and S1617K, are found in lVS3-S4 constituting receptor site-3, and for receptor site-4, two residues (Leu-Pro) are inserted near IIS4 of scorpion sodium channel. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
收录类别 | SCI |
语种 | 英语 |
公开日期 | 2013-09-17 |
源URL | [http://ir.iphy.ac.cn/handle/311004/34937] ![]() |
专题 | 物理研究所_物理所公开发表论文_物理所公开发表论文_期刊论文 |
推荐引用方式 GB/T 7714 | Zuo, XP,He, HQ,He, M,et al. Comparative pharmacology and cloning of two novel arachnid sodium channels: Exploring the adaptive insensitivity of scorpion to its toxins[J]. FEBS LETTERS,2006,580(18):4508. |
APA | Zuo, XP.,He, HQ.,He, M.,Liu, ZR.,Xu, Q.,...&Ji, YH.(2006).Comparative pharmacology and cloning of two novel arachnid sodium channels: Exploring the adaptive insensitivity of scorpion to its toxins.FEBS LETTERS,580(18),4508. |
MLA | Zuo, XP,et al."Comparative pharmacology and cloning of two novel arachnid sodium channels: Exploring the adaptive insensitivity of scorpion to its toxins".FEBS LETTERS 580.18(2006):4508. |
入库方式: OAI收割
来源:物理研究所
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