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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation

  • Park, Young-Hoon (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jeong, Suk (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Ha, Ki-Tae (Department of Korean Medical Science, School of Korean Medicine and Korean Medicine Research Centre for Healthy Aging, Pusan National University) ;
  • Yu, Hak Sun (Department of Parasitology, School of Medicine, Pusan National University) ;
  • Jang, Se Bok (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • Received : 2016.12.05
  • Accepted : 2017.03.29
  • Published : 2017.05.31
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Abstract

The biological activities of macrophage migration inhibitory factor (MIF) might be mediated through a classical receptor-mediated or non-classical endocytic pathway. JAB1 (C-Jun activation domain-binding protein-1) promotes the degradation of the tumor suppressor, p53, and the cyclin-dependent kinase inhibitor, p27. When MIF and JAB1 are bound to each other in various intracellular sites, MIF inhibits the positive regulatory effects of JAB1 on the activity of AP-1. The intestinal parasite, Anisakis simplex, has an immunomodulatory effect. The molecular mechanism of action of As-MIF and human JAB1 are poorly understood. In this study, As-MIF and hJAB1 were expressed and purified with high solubility. The structure of As-MIF and hJAB1 interaction was modeled by homology modeling based on the structure of Ace-MIF. This study provides evidence indicating that the MIF domain of As-MIF interacts directly with the MPN domain of hJAB1, and four structure-based mutants of As-MIF and hJAB1 disrupt the As-MIF-hJAB1 interaction.

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References

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