NDLI: Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family.

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Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family.

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Crystal structure of calcium-free human sorcin: a member of the penta-EF-hand protein family.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Swenson, L. Dwyer, M. D. Xie, X. Parker, M. H. Botfield, M. C.
Description	Country affiliation: United States Author Affiliation: Xie X ( Vertex Pharmaceuticals Incorporated, Cambridge, Massachusetts 02139-4211, USA. xiaoling_xie@vpharm.com)
Abstract	Sorcin is a 22 kD calcium-binding protein that is found in a wide variety of cell types, such as heart, muscle, brain and adrenal medulla. It belongs to the penta-EF-hand (PEF) protein family, which contains five EF-hand motifs that associate with membranes in a calcium-dependent manner. Prototypic members of this family are the calcium-binding domains of calpain, such as calpain dVI. Full-length human sorcin has been crystallized in the absence of calcium and the structure determined at 2.2 A resolution. Apart from an extended N-terminal portion, the sorcin molecule has a globular shape. The C-terminal domain is predominantly alpha-helical, containing eight alpha-helices and connecting loops incorporating five EF hands. Sorcin forms dimers through the association of the unpaired EF5, confirming this as the mode of association in the dimerization of PEF proteins. Comparison with calpain dVI reveals that the general folds of the individual EF-hand motifs are conserved, especially that of EF1, the novel EF-hand motif characteristic of the family. Detailed structural comparisons of sorcin with other members of PEF indicate that the EF-hand pair EF1-EF2 is likely to correspond to the two physiologically relevant calcium-binding sites and that the calcium-induced conformational change may be modest and localized within this pair of EF-hands. Overall, the results derived from the structural observations support the view that, in sorcin, calcium signaling takes place through the first pair of EF-hands.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium-binding Proteins Chemistry Amino Acid Motifs Amino Acid Sequence Annexins Calpain Crystallography, X-ray Dimerization Ef Hand Motifs Models, Molecular Molecular Sequence Data Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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