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NMR-derived solution structure of the C-terminal domain of Calcium Vector Protein (from Amphioxus) in the Ca2+-bound form
NMR-derived solution structure of the C-terminal domain of Calcium Vector Protein (from Amphioxus) in the Ca2+-bound form [1]. In absence of calcium the domain is highly flexible, having properties of a molten globule. The first Ca2+ ion binds to the first ion-binding site, while the second site is still fluctuating. The two (Ca2+)2 -bound form sown in the figure) has an "open" structure, characteristic of Ca2+ sensors of the EF-hand family. This represents a novel metal-induced structural rearrangement within the EF-hand family.
[1] Théret, I., et al., Sequential calcium binding to the regulatory domain of Calcium Vector Protein reveals functional assymmetry and is accompanied by large structural changes. Biochemistry (2000), 39, 7920-7926.