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- W78209491 abstract "Calmodulin (CaM) is an acidic protein of 148 amino acid residues that plays a central role in cellular regulation by relating the levels of cellular calcium to the activities of regulatory proteins, such as kinases, phosphatases, etc. Recent studies with synthetic models and natural peptides have shown that CaM recognizes positively charged, amphiphilic peptides [1]. There is no exact sequence homology in the CaM binding proteins, but they frequently contain segments rich in basic residues (Arg, Lys, His) and are capable of adopting, when they bind to CaM, an amphiphilic conformation. These observations demonstrated that this structural feature is important for binding, and that hydrophobic and electrostatic interactions both play a relevant role. We report here our approach for the design of an dimer covalently linked in a parallel or antiparallel orientation that is able to specifically interact with only one of the target enzymes recognized by CaM and form three stranded coiled coils. The target sequence that we chose for binding was the CaM binding domain of calcineurin. This important enzyme is the target of immunosuppressive drugs, such as cyclosporin A and FK506. A peptide that specifically binds to calcineurin could be expected to be either an immune-stimulant or an immune-suppressant, depending on whether it activates or inhibits activation of the enzyme." @default.
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- W78209491 date "2005-12-02" @default.
- W78209491 modified "2023-10-17" @default.
- W78209491 title "A novel class of Calmodulin mimetics: De Novo designed proteins in molecular recognition" @default.
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- W78209491 doi "https://doi.org/10.1007/0-306-46862-x_32" @default.
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