TYR(13) IS ESSENTIAL FOR THE BINDING OF OMEGA-CONOTOXIN-MVIIC TO THE P/Q-TYPE CALCIUM-CHANNEL

被引：17
作者：
KIM, JI
TAKAHASHI, M
MARTINMOUTOT, N
SEAGAR, MJ
OHTAKE, A
SATO, K
机构：
[1] MITSUBISHI KASEI INST LIFE SCI, MACHIDA 194, TOKYO, JAPAN
[2] FAC MED SECTEUR NORD MARSEILLE, INST JEAN ROCHE, INSERM, U374, F-13926 MARSEILLE 20, FRANCE
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 214卷 / 02期
关键词：
D O I：
10.1006/bbrc.1995.2288
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：
An analog of omega-conotoxin MVIIC (Y13A-MVIIC) was synthesized by replacing Tyr(13) with Ala to study the role of Tyr(13) residue conserved in many omega-conotoxins. Y13A-MVIIC has an overall conformation similar to that of the native toxin, but an enormously reduced ability to displace I-125-omega-conotoxin MVIIC binding to rat cerebellar P2 membranes. These results suggest that Tyr(13) is essential for the activity of omega-conotoxins at P/Q-type calcium channels. (C) 1995 Academic Press, Inc.
引用
收藏
页码：305 / 309
页数：5
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