Structural characterization of As-MIF and hJAB1 during the inhibition of cell-cycle regulation.

Abstract:

:The biological activities of macrophage migration inhibitory factor (MIF) might be mediated through a classical receptormediated 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. [BMB Reports 2017; 50(5): 269-274].

journal_name

BMB Rep

journal_title

BMB reports

authors

Park YH,Jeong MS,Ha KT,Yu HS,Jang SB

doi

10.5483/bmbrep.2017.50.5.201

subject

Has Abstract

pub_date

2017-05-01 00:00:00

pages

269-274

issue

5

eissn

1976-6696

issn

1976-670X

pii

3718

journal_volume

50

pub_type

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