BMB Reports Papers in Press available online.

Search Papers In Press
This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation
Young-Hoon Park1,#, Mi Suk Jeong1,#, Ki-Tae Ha2, Hak Sun Yu3, Se Bok Jang1,*
1Department of Molecular Biology, College of Natural Sciences, and 2Department of Korean Medical Science, School of Korean Medicine and Korean Medicine Research Centre, Pusan National University,
3Department of Parasitology, School of Medicine, School of Medicine, Pusan National University
Macrophage migration inhibitory factor (MIF) might mediate its biological activities through a classical receptor-mediated or non-classical endocytic pathway. JAB1 (C-Jun activation domain-binding protein-1) promotes degradation of the tumor suppressor p53 and the cyclin-dependent kinase inhibitor p27. When MIF and JAB1 are bound to each other in 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 proteins remain poorly understood. In this study, As-MIF and hJAB1 were successfully expressed and purified with high solubility. We modeled the 3D structure of As-MIF and its interaction with hJAB1 by homology modeling based on the structure of the Ace-MIF. We provide 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 disrupted the As-MIF-hJAB1 interaction.
Abstract, Accepted Manuscript(in press) [Submitted on December 5, 2016, Accepted on March 29, 2017]
  Copyright © KSBMB. All rights reserved. / Powered by, Ltd