Structural probing of Zn(II), Cd(II) and Hg(II) binding to human ubiquitin

被引：25

作者：

Falini, Giuseppe ^{[1
]}

Fermani, Simona ^{[1
]}

Tosi, Giovanna ^{[1
]}

Arnesano, Fabio ^{[2
]}

Natile, Giovanni ^{[2
]}

机构：

[1] Univ Bologna, Dipartimento Chim G Ciamician, I-40126 Bologna, Italy

[2] Univ Bari A Moro, Dipartimento Farmacochim, I-70125 Bari, Italy

来源：

CHEMICAL COMMUNICATIONS | 2008年 / 45期

关键词：

D O I：

10.1039/b813463d

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A structural investigation performed on adducts of human ubiquitin with group-12 metal ions reveals common preferential anchoring sites, the most populated one being His68; at higher metal ion concentration a second and a third site, close to the N-terminus of the protein, become populated and promote a polymorphic transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the latter metal binding, undergo a remarkable displacement from their position in native ubiquitin; the aggregate stereochemistry appears to be driven by the clustering of deshielded backbone hydrogen-bond patches, and metal ions foster this process.

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收藏

页码：5960 / 5962

页数：3

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