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Issue 12, 2017
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Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic

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Abstract

Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acute-phase protein and a free radical scavenger. The structural organization of Cp causes its sensitivity to proteolysis and ROS (reactive oxygen species), which can alter some of the important Cp functions. Elucidation of the orthorhombic crystal structure of rat Cp at 2.3 Å resolution revealed the basis for stronger resistance of rat Cp to proteolysis and a new labile copper binding site. The presence of this site appears as a very rare and distinctive feature of rat Cp as was shown by sequence alignment of ceruloplasmin, hephaestin and zyklopen in the Deuterostomia taxonomic group. The trigonal crystal form of rat Cp at 3.2 Å demonstrates unexpected partial substitution of copper by zinc.

Graphical abstract: Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic

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Article information


Submitted
17 May 2017
Accepted
14 Nov 2017
First published
14 Nov 2017

Metallomics, 2017,9, 1828-1838
Article type
Paper

Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic

V. R. Samygina, A. V. Sokolov, G. Bourenkov, T. R. Schneider, V. A. Anashkin, S. O. Kozlov, N. N. Kolmakov and V. B. Vasilyev, Metallomics, 2017, 9, 1828
DOI: 10.1039/C7MT00157F

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