| Literature DB >> 16732294 |
Lucia Banci1, Ivano Bertini, Francesca Cantini, Isabella C Felli, Leonardo Gonnelli, Nick Hadjiliadis, Roberta Pierattelli, Antonio Rosato, Petros Voulgaris.
Abstract
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.Entities:
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Year: 2006 PMID: 16732294 DOI: 10.1038/nchembio797
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040