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KMID : 0624620170500050269
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BMB Reports
2017 Volume.50 No. 5 p.269 ~ p.274
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Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation
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Park Young-Hoon
Jeong Mi-Suk
Ha Ki-Tae
Yu Hak-Sun
Jang Se-Bok
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Abstract
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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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KEYWORD
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As-MIF, Cell-cycle, hJAB1, Molecular interaction, Mutations
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