http://www.cnr.it/ontology/cnr/individuo/prodotto/ID11626

Structure-function relationships in sorcin, a member of the penta EF-hand family. Interaction of sorcin fragments with the ryanodine receptor and an Escherichia coli model system. (Articolo in rivista)

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Structure-function relationships in sorcin, a member of the penta EF-hand family. Interaction of sorcin fragments with the ryanodine receptor and an Escherichia coli model system. (Articolo in rivista) (literal)

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Zamparelli C; Ilari A; Verzili D; Giangiacomo L; Colotti G; Pascarella S; Chiancone E. (2000)
Structure-function relationships in sorcin, a member of the penta EF-hand family. Interaction of sorcin fragments with the ryanodine receptor and an Escherichia coli model system.
in Biochemistry (Easton); ACS, American chemical society, Washington, DC (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Zamparelli C; Ilari A; Verzili D; Giangiacomo L; Colotti G; Pascarella S; Chiancone E. (literal)

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Univ Rome La Sapienza, CNR, Ctr Mol Biol, Dept Biochem Sci A Rossi Fanelli, I-00185 Rome, Italy (literal)

Titolo

Structure-function relationships in sorcin, a member of the penta EF-hand family. Interaction of sorcin fragments with the ryanodine receptor and an Escherichia coli model system. (literal)

Abstract

Sorcin, a 21.6 kDa cytosolic EF-hand protein which undergoes a Ca2+-induced translocation from cytoplasm to membranes, has been assigned to the newly defined penta EF-hand family. A molecular model of the C-terminal Ca2+-binding domain has been generated using as a template the X-ray coordinates of the corresponding domain in the calpain light subunit, the family prototype [Lin, G., et al. (1997) Nat. Struct. Biol. 4, 539-546]. The model indicates that in sorcin the three-dimensional structure is conserved and in particular that of EF1, the novel EF-hand motif characteristic of the family. On this basis, two stable fragments have been obtained and characterized. Just like the native protein, the sorcin Ca2+- binding domain (residues 33-198) is largely dimeric, interacts with the ryanodine receptor at physiological calcium concentrations, and undergoes a reversible, Ca2+-dependent translocation from cytosol to target proteins on Escherichia coli membranes. In contrast, the 90-198 fragment (residues 90-198), which lacks EF1 and EF2, does not bind Ca2+ with high affinity and is unable to translocate. Binding of calcium to the EF1-EF2 pair is therefore required for the activation of sorcin which uses the C-terminal calcium-binding domain for interaction with the ryanodine receptor, a physiological target in muscle cells. (literal)

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