The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein

Autor: Ilari A (1), Johnson KA (2), Nastopoulos V (3), Verzili D (1), Zamparelli C (2), Colotti G (1), Tsernoglou D (2), Chiancone E. (1

Publikováno v: Journal of Molecular Biology 29 (2002): 447–458.
info:cnr-pdr/source/autori:Ilari A (1), Johnson KA (2), Nastopoulos V (3), Verzili D (1), Zamparelli C (2), Colotti G (1), Tsernoglou D (2), Chiancone E. (1,2)/titolo:The crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length protein/doi:/rivista:Journal of Molecular Biology/anno:2002/pagina_da:447/pagina_a:458/intervallo_pagine:447–458/volume:29

Sorcin is a 21.6 kDa calcium binding protein, expressed in a number of mammalian tissues that belongs to the small, recently identified penta-EF-hand (PEF) family. Like all members of this family, sorcin undergoes a Ca2+-dependent translocation from

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https://publications.cnr.it/doc/11344