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

被引：16

作者：

Samygina, V. R. ^{[1
,2
]}

Sokolov, A. V. ^{[3
,4
,5
]}

Bourenkov, G. ^{[6
]}

Schneider, T. R. ^{[6
]}

Anashkin, V. A. ^{[1
,7
,8
]}

Kozlov, S. O. ^{[3
]}

Kolmakov, N. N. ^{[3
]}

Vasilyev, V. B. ^{[3
,4
]}

机构：

[1] Shubnikov Inst Crystallog FSRC Crystallog & Photo, Leninsky Pr 59, Moscow 117333, Russia

[2] NRC Kurchatov Inst, Kurchatov Pl 1, Moscow 123098, Russia

[3] Inst Expt Med, Ul Acad Pavlova 12, St Petersburg 199034, Russia

[4] St Petersburg State Univ, Univ Nab 7-9, St Petersburg 199034, Russia

[5] Almazov Natl Med Res Ctr, Ctr Preclin Translat Res, Ul Dolgoozernaya 43, St Petersburg 197371, Russia

[6] EMBL, Notkestr 85, D-22607 Hamburg, Germany

[7] Lomonosov Moscow State Univ, Belozersky Inst Physicochem Biol, Moscow 119899, Russia

[8] Lomonosov Moscow State Univ, Dept Chem, Moscow 119899, Russia

来源：

METALLOMICS | 2017年 / 9卷 / 12期

关键词：

SERUM CERULOPLASMIN; MYELOPEROXIDASE; IDENTIFICATION; PLASMA; ZINC; COMPONENTS; PROTEIN; MODEL;

D O I：

10.1039/c7mt00157f

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：

Ceruloplasmin (Cp) is a copper-containing multifunctional oxidase of plasma, an antioxidant, an acutephase 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 angstrom 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 angstrom demonstrates unexpected partial substitution of copper by zinc.

引用

页码：1828 / 1838

页数：11

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