Low-resolution structural studies of human Stanniocalcin-1 |
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Authors: | Daniel M Trindade Júlio C Silva Margareth S Navarro Iris CL Torriani Jörg Kobarg |
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Affiliation: | 1. Centro de Biologia Molecular Estrutural (CEBIME), Campinas, SP, Brazil 2. Instituto de Biologia, Departamento de Bioquímica, Universidade Estadual de Campinas, Campinas, SP, Brazil 3. Instituto de Física "Gleb Wataghin", Universidade Estadual de Campinas, Campinas, SP, Brazil 4. Laboratório Nacional de Luz Síncrotron (LNLS), Campinas, SP, Brazil
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Abstract: | Background Stanniocalcins (STCs) represent small glycoprotein hormones, found in all vertebrates, which have been functionally implicated in Calcium homeostasis. However, recent data from mammalian systems indicated that they may be also involved in embryogenesis, tumorigenesis and in the context of the latter especially in angiogenesis. Human STC1 is a 247 amino acids protein with a predicted molecular mass of 27 kDa, but preliminary data suggested its di- or multimerization. The latter in conjunction with alternative splicing and/or post-translational modification gives rise to forms described as STC50 and "big STC", which molecular weights range from 56 to 135 kDa. |
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