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精氨酸481突变消除了AMPA选择性谷氨酸受体通道α1亚基的配体结合。

Arginine-481 mutation abolishes ligand-binding of the AMPA-selective glutamate receptor channel alpha1-subunit.

作者信息

Kawamoto S, Uchino S, Xin K Q, Hattori S, Hamajima K, Fukushima J, Mishina M, Okuda K

机构信息

Department of Bacteriology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama, Japan.

出版信息

Brain Res Mol Brain Res. 1997 Jul;47(1-2):339-44. doi: 10.1016/s0169-328x(97)00103-4.

DOI:10.1016/s0169-328x(97)00103-4
PMID:9221933
Abstract

Arginine-481 is located in the putative agonist-binding region preceding the putative transmembrane segment M1 of the alpha1-subunit of the AMPA-selective glutamate receptor (GluR) channel. This amino acid is completely conserved among GluR proteins. A site-directed mutagenesis study using a baculovirus expression system showed that substitution of glutamate, glutamine and lysine for arginine-481 of the recombinant alpha1-subunit protein abolishes binding to [3H]AMPA completely. The present study provides the first direct experimental evidence that the conserved charged arginine-481 residue is essential, directly or indirectly, for the acquisition of ligand-binding activity by the receptor protein.

摘要

精氨酸 - 481位于AMPA选择性谷氨酸受体（GluR）通道α1亚基假定跨膜片段M1之前的假定激动剂结合区域。该氨基酸在GluR蛋白中完全保守。一项使用杆状病毒表达系统的定点诱变研究表明，用谷氨酸、谷氨酰胺和赖氨酸取代重组α1亚基蛋白的精氨酸 - 481会完全消除与[3H]AMPA的结合。本研究提供了首个直接实验证据，即保守的带电荷精氨酸 - 481残基直接或间接对于受体蛋白获得配体结合活性至关重要。

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