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
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.
引用
收藏
页码:5960 / 5962
页数:3
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