NICOTINIC RECEPTOR-BINDING SITE PROBED WITH UNNATURAL AMINO-ACID-INCORPORATION IN INTACT-CELLS

被引：213

作者：

NOWAK, MW ^{[1
]}

KEARNEY, PC

SAMPSON, JR

SAKS, ME

LABARCA, CG

SILVERMAN, SK

ZHONG, W

THORSON, JS

ABELSON, JN

DAVIDSON, N

SCHULTZ, PG

DOUGHERTY, DA

LESTER, HA

机构：

[1] CALTECH, DIV BIOL, PASADENA, CA 91125 USA

[2] CALTECH, DIV CHEM & CHEM ENGN, PASADENA, CA 91125 USA

[3] UNIV CALIF BERKELEY, HOWARD HUGHES MED INST, DEPT CHEM, BERKELEY, CA 94720 USA

来源：

SCIENCE | 1995年 / 268卷 / 5209期

关键词：

D O I：

10.1126/science.7716551

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The nonsense codon suppression method for unnatural amino acid incorporation has been applied to intact Cells and combined with electrophysiological analysis to probe structure-function relations in the nicotinic acetylcholine receptor, Functional receptors were expressed in Xenopus oocytes when tyrosine and phenylalanine derivatives were incorporated at positions 93, 190, and 198 in the binding site of the a subunit, Subtle changes in the structure of an individual side chain produced readily detectable changes in the function of this large channel protein, At each position, distinct features of side chain structure dominated the dose-response relation, probably by governing the agonist-receptor binding.

引用

页码：439 / 442

页数：4

共 42 条

[1]

ABRAMSON SN, 1989, J BIOL CHEM, V264, P12666

[2] ACETYLCHOLINE-RECEPTOR KINETICS [J].