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  • Title: Modeling studies on the structural determinants for the DAG/phorbol ester binding to C1 domain.
    Author: Rahman GM, Das J.
    Journal: J Biomol Struct Dyn; 2015; 33(1):219-32. PubMed ID: 24666138.
    Abstract:
    C1 domains are small zinc-binding structural units of approximately 50 amino acids, originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to the DAG/phorbol ester are termed as typical, and those that do not respond to DAG/phorbol ester are termed as atypical. To design molecules targeting a specific C1 domain for regulating a specific disease state, it is important to understand the factors that make a C1 domain responsive to DAG/phorbol ester. Here, we determined the volume and surface area of the ligand-binding site for all known C1 domains. No correlation was found between the volume/surface area of ligand-binding site and the DAG/phorbol ester-binding affinity. Solvated molecular dynamics simulation reveals that the presence of water molecules affects the flexibility of the ligand-binding site. Contributions of the binding site residues, their orientations, and the membrane lipids on the responsiveness of a C1 domain towards DAG/phorbol ester have been discussed.
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