NMR and mutagenesis of human copper transporter 1 (hCtr1) show that Cys-189 is required for correct folding and dimerization

被引：7

作者：

Lee, Sangwon ^{[1
,2
]}

Howell, Stephen B. ^{[1
,2
]}

Opella, Stanley J. ^{[1
,2
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2007年 / 1768卷 / 12期

关键词：

oligomerization; copper transport; hCtr1; NMR; disulfide bond;

D O I：

10.1016/j.bbamem.2007.08.037

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 human high-affinity copper transporter (hCtr1) is a membrane protein that is predicted to have three transmembrane helices and two methionine-rich metal binding motifs. As an oligomeric polytopic membrane protein, hCtrl is a challenging system for experimental structure determination. The results of an initial application of solution-state NMR methods to a truncated construct containing residues 45-190 in micelles and site-directed mutagenesis of the two cysteine residues demonstrate that Cys-189 but not Cys-161 is essential for both dimer formation and proper folding of the protein. (C) 2007 Elsevier B.V. All rights reserved.

引用

页码：3127 / 3134

页数：8

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