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Open Access Intracellular Calcium-Binding Proteins in Signal Transduction

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Cell stimulation generates a Ca2+ signal, which is perceived by intracellular Ca2+-binding proteins. These proteins are made up of different units of a conserved structural motif, called the 2S domain, and composed mainly of four β-helices and two anti parallel β-strands. This 2S domain can bind 2 Ca2+ ions and is roughly cup-shaped in the Ca2+-bound configuration. The interior of the cup is lined with solvent-exposed hydrophobic residues. In Ca2+-binding proteins involved in cellular signal-response coupling, such as calmodulin and troponin C, the hydrophobic cup is essential for interaction with, and activation of the response proteins. The Ca2+-free state is characterized by a reorientation of the β-helices and shielding of the hydrophobic residues in the cup. In contrast, interaction with the target strongly stabilizes the hydrophobic cups. Ca2+-buffering proteins, such as parvalbumin and sarcoplasmic Ca2+-binding proteins, have intrinsically a stable conformation, since the strongly hydrophobic cups are stabilized by frontal self association of the 2S domains.

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Document Type: Research Article

Publication date: April 1, 1992

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  • International Journal for Chemistry and Official Membership Journal of the Swiss Chemical Society (SCS) and its Divisions

    CHIMIA, a scientific journal for chemistry in the broadest sense, is published 10 times a year and covers the interests of a wide and diverse readership. Contributions from all fields of chemistry and related areas are considered for publication in the form of Review Articles and Notes. A characteristic feature of CHIMIA are the thematic issues, each devoted to an area of great current significance.

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