The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction

被引：181

作者：

Banci, Lucia

Bertini, Ivano

Cantini, Francesca

Felli, Isabella C.

Gonnelli, Leonardo

Hadjiliadis, Nick

Pierattelli, Roberta

Rosato, Antonio

Voulgaris, Petros

机构：

[1] Univ Florence, Magnet Resonance Ctr, CERM, I-50019 Sesto Fiorentino, Italy

[2] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy

[3] Univ Ioannina, Dept Chem, Sect Inorgan & Analyt Chem, GR-45110 Ioannina, Greece

来源：

NATURE CHEMICAL BIOLOGY | 2006年 / 2卷 / 07期

关键词：

D O I：

10.1038/nchembio797

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：

Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.

引用

页码：367 / 368

页数：2

共 14 条

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