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http://dx.doi.org/10.5483/BMBRep.2017.50.5.201

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)
Publication Information
BMB Reports / v.50, no.5, 2017 , pp. 269-274 More about this Journal
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.
Keywords
As-MIF; Cell-cycle; hJAB1; Molecular interaction; Mutations;
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