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Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic
Metallomics ( IF 3.4 ) Pub Date : 2017-11-14 00:00:00 , DOI: 10.1039/c7mt00157f
V. R. Samygina 1, 2, 3, 4, 5 , A. V. Sokolov 4, 6, 7, 8, 9 , G. Bourenkov 10, 11, 12, 13 , T. R. Schneider 10, 11, 12, 13 , V. A. Anashkin 1, 2, 3, 4, 14 , S. O. Kozlov 4, 6, 7, 8 , N. N. Kolmakov 4, 6, 7, 8 , V. B. Vasilyev 4, 6, 7, 8, 9
Affiliation  

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.

中文翻译:

大鼠铜蓝蛋白:新的不稳定的铜结合位点和锌/铜镶嵌

铜蓝蛋白(Cp)是血浆中的含铜多功能氧化酶,抗氧化剂,急性期蛋白和自由基清除剂。Cp的结构组织使其对蛋白水解和ROS(活性氧)敏感,这可能会改变某些重要的Cp功能。以2.3Å分辨率阐明大鼠Cp的斜方晶体结构,揭示了大鼠Cp对蛋白水解的更强抗性和新的不稳定的铜结合位点的基础。如通过血浆铜蓝蛋白,hephaestin的序列比对所示和所zyklopen此位点的存在显示为大鼠Cp的一种非常罕见的和显着的特征Deuterostomia分类组。大鼠Cp在3.2Å处的三角晶形表明铜被锌意外地部分取代。
更新日期:2017-11-27
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