酪氨酸13对于ω-芋螺毒素MVIIC与P/Q型钙通道的结合至关重要。

Tyr13 is essential for the binding of omega-conotoxin MVIIC to the P/Q-type calcium channel.

作者信息

Kim J I, Takahashi M, Martin-Moutot N, Seagar M J, Ohtake A, Sato K

机构信息

Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.

出版信息

Biochem Biophys Res Commun. 1995 Sep 14;214(2):305-9. doi: 10.1006/bbrc.1995.2288.

DOI:10.1006/bbrc.1995.2288

PMID:7677735

Abstract

An analog of omega-conotoxin MVIIC (Y13A-MVIIC) was synthesized by replacing Tyr13 with Ala to study the role of Tyr13 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 125I-omega-conotoxin MVIIC binding to rat cerebellar P2 membranes. These results suggest that Tyr13 is essential for the activity of omega-conotoxins at P/Q-type calcium channels.

摘要

通过将酪氨酸13（Tyr13）替换为丙氨酸（Ala）合成了ω-芋螺毒素MVIIC（Y13A-MVIIC）的类似物，以研究在许多ω-芋螺毒素中保守的Tyr13残基的作用。Y13A-MVIIC的整体构象与天然毒素相似，但取代125I-ω-芋螺毒素MVIIC与大鼠小脑P2膜结合的能力大大降低。这些结果表明，Tyr13对于ω-芋螺毒素在P/Q型钙通道上的活性至关重要。