Solution structure of α-conotoxin ImI determined by two-dimensional NMR spectroscopy

被引：14

作者：

Gouda, H ^{[1
]}

Hirono, S ^{[1
]}

机构：

[1] Kitasato Univ, Sch Pharmaceut Sci, Minato Ku, Tokyo 1088641, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1431卷 / 02期

关键词：

solution structure; neurotoxin; two-dimensional nuclear magnetic resonance; acetylcholine receptor; Conus imperialis;

D O I：

10.1016/S0167-4838(99)00065-5

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：

The three-dimensional structure of alpha-conotoxin ImI, a potent antagonist targeting the neuronal alpha 7 subtype of nicotinic acetylcholine receptor (nAChR), has been investigated by NMR spectroscopy. On the basis of 181 experimental constraints, a total of 25 converged structures were obtained. The average pairwise atomic root mean square difference is 0.40 +/- 0.11 Angstrom for the backbone atoms. The resulting structure indicates the presence of two successive type I beta-turns and a 3(10) helix for residues Cys2-Cys8 and Ala9-Arg11, respectively, and shows a significant structural similarity to that of alpha-conotoxin PnIA, which is also selective for the neuronal nAChR. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：384 / 394

页数：11

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