![]() ![]() ![]() By analyzing the interactions, Ser 15, Lys 32 had significant interactions with selected ligand molecules and Val5, which may have hydrophobic interaction with the cyclic group of the ligand. As a result of docking, a list of compounds was shown good inhibiting properties with target protein. A total of 133 analog compounds of existing drugs for scorpion bites were used for docking. Results: The predicted structure has 91.7% of amino acids in the core and allowed regions of Ramachandran plot. The amino acid residues lining the binding site were predicted and used for toxin-ligand docking studies, further, selected toxin-inhibitor complexes were studied using molecular dynamics (MD) simulations. Materials and Methods: The structure of ChTx-C was modeled using Modeller 9v7. Detailed understanding the structure of ChTx-C, conformational stability, and intermolecular interactions are required to select the potential inhibitors of the toxin. Objective: Charybdotoxin-C (ChTx-C), from the scorpion Leiurus, quinquestriatus hebraeus blocks the calcium-activated potassium channels and causes hyper excitability of the nervous system.
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