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Rat ceruloplasmin: a new labile copper binding site and zinc/copper mosaic.
Samygina, V R; Sokolov, A V; Bourenkov, G; Schneider, T R; Anashkin, V A; Kozlov, S O; Kolmakov, N N; Vasilyev, V B.
Afiliación
  • Samygina VR; Shubnikov Institute of Crystallography of FSRC "Crystallography and Photonics" RAS, Leninsky pr.59, Moscow 117333, Russia. lera@ns.crys.ras.ru and NRC Kurchatov Institute, Kurchatov pl. 1, Moscow 123098, Russia.
  • Sokolov AV; Institute of Experimental Medicine, ul. Academica Pavlova, 12, Saint-Petersburg 197376, Russia and Saint-Petersburg State Universisty, Universitetskaya nab. 7-9, Saint-Petersburg 199034, Russia and Centre of Preclinical Translational Research, Almazov National Medical Research Centre, ul. Dolgoozern
  • Bourenkov G; EMBL, Notkestrasse 85, 22607 Hamburg, Germany.
  • Schneider TR; EMBL, Notkestrasse 85, 22607 Hamburg, Germany.
  • Anashkin VA; Shubnikov Institute of Crystallography of FSRC "Crystallography and Photonics" RAS, Leninsky pr.59, Moscow 117333, Russia. lera@ns.crys.ras.ru and Belozersky Institute of Physico-Chemical Biology and Department of Chemistry, Lomonosov Moscow State University, Moscow 119899, Russia.
  • Kozlov SO; Institute of Experimental Medicine, ul. Academica Pavlova, 12, Saint-Petersburg 197376, Russia.
  • Kolmakov NN; Institute of Experimental Medicine, ul. Academica Pavlova, 12, Saint-Petersburg 197376, Russia.
  • Vasilyev VB; Institute of Experimental Medicine, ul. Academica Pavlova, 12, Saint-Petersburg 197376, Russia and Saint-Petersburg State Universisty, Universitetskaya nab. 7-9, Saint-Petersburg 199034, Russia.
Metallomics ; 9(12): 1828-1838, 2017 12 01.
Article en En | MEDLINE | ID: mdl-29177316
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Zinc / Ceruloplasmina / Cobre Límite: Animals / Humans Idioma: En Revista: Metallomics Asunto de la revista: BIOQUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Zinc / Ceruloplasmina / Cobre Límite: Animals / Humans Idioma: En Revista: Metallomics Asunto de la revista: BIOQUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Reino Unido