SOLUTION STRUCTURE OF OMEGA-CONOTOXIN MVIIA USING 2D NMR-SPECTROSCOPY

被引：65

作者：

BASUS, VJ ^{[1
]}

NADASDI, L ^{[1
]}

RAMACHANDRAN, J ^{[1
]}

MILJANICH, GP ^{[1
]}

机构：

[1] NEUREX CORP, MENLO PK, CA 94025 USA

来源：

FEBS LETTERS | 1995年 / 370卷 / 03期

基金：

美国国家科学基金会;

关键词：

NEUROTOXIN; CALCIUM CHANNEL BLOCKER; NMR STRUCTURE; COMPLETE RELAXATION MATRIX; CONUS MAGUS;

D O I：

10.1016/0014-5793(95)00819-U

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 solution structure of omega-conotoxin MVIIA (SNX-111), a peptide toxin from the fish hunting cone snail Conus magus and a high-affinity blocker of N-type calcium channels, was determined by 2D NMR spectroscopy. The backbones of the best 44 structures match with an average pairwise RMSD of 0.59 angstroms. The structures contain a short segment of triple-stranded beta-sheet involving residues 6-8, 20-21, and 24-25. The structure of this toxin is very similar to that of omega-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.

引用

页码：163 / 169

页数：7

共 46 条

[1]

BASUS VJ, 1989, METHOD ENZYMOL, V177, P132

[2] MLEV-17-BASED TWO-DIMENSIONAL HOMONUCLEAR MAGNETIZATION TRANSFER SPECTROSCOPY [J].