Stabilizing effect of Zn2+ in native bovine rhodopsin

被引：54

作者：

Park, Paul S. -H.

Sapra, K. Tanuj

Kolinski, Michal

Filipek, Slawomir

Palczewski, Krzysztof

Muller, Daniel J.

机构：

[1] Case Western Reserve Univ, Dept Pharmacol, Cleveland, OH 44106 USA

[2] Univ Technol, Ctr Biotechnol, D-01307 Dresden, Germany

[3] Int Inst Mol & Cell Biol, PL-02109 Warsaw, Poland

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2007年 / 282卷 / 15期

关键词：

D O I：

10.1074/jbc.M610341200

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：

Single-molecule force spectroscopy ( SMFS) is a powerful tool to dissect molecular interactions that govern the stability and function of proteins. We applied SMFS to understand the effect of Zn2+ on the molecular interactions underlying the structure of rhodopsin. Force-distance curves obtained from SMFS assays revealed the strength and location of molecular interactions that stabilize structural segments within this receptor. The inclusion of ZnCl2 inSMFSassay buffer increased the stability of most structural segments. This effect was not mimicked by CaCl2, CdCl2, or CoCl2. Thus, Zn2+ stabilizes the structure of rhodopsin in a specific manner.

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收藏

页码：11377 / 11385

页数：9

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