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  • Title: Purification, characterization and docking studies of the HIN domain of human myeloid nuclear differentiation antigen (MNDA).
    Author: Li H, Wang ZX, Wu JW.
    Journal: Biotechnol Lett; 2014 May; 36(5):899-905. PubMed ID: 24557068.
    Abstract:
    The HIN domain of myeloid nuclear differentiation antigen (MNDA) was expressed and purified as a monomer using E. coli JM109 as host. The protein interacted with double-stranded DNA at a Kd of 3.15 μM and did not recognize the termini of double-stranded DNA. Isothermal titration calorimetry indicated that the interaction between the protein and double-stranded DNA is mainly mediated by electrostatic attractions and hydrogen bonding. We developed a model to analyze the potential DNA binding site of the MNDA HIN domain. Based on the model, molecular docking and mutation studies suggest that the double-stranded DNA binding site of the protein is different from other HIN-DNA structures. This work facilitates the design of specific drugs against pathogens detected by human MNDA.
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