Open AccessCharacterization of the amino-terminal domain of Mx2/MxB-dependent interaction with the HIV-1 capsid
Author(s) -
Jia Kong,
Bo Xu,
Wei Wei,
Xin Wang,
Wei Xie,
Xiao-Fang Yu
Publication year - 2014
Publication title -
protein and cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.973
H-Index - 63
eISSN - 1674-8018
pISSN - 1674-800X
DOI - 10.1007/s13238-014-0113-5
Subject(s) - capsid , human immunodeficiency virus (hiv) , human genetics , terminal (telecommunication) , biology , developmental biology , domain (mathematical analysis) , characterization (materials science) , genetics , computational biology , microbiology and biotechnology , virology , virus , computer science , nanotechnology , materials science , telecommunications , mathematics , gene , mathematical analysis
Figure S1 Architecture of the Mx2 constucts. (A) Structure-based domain representation of human Mx2 constructs. Wild-type human MxA and Mx2 are depicted in the top figure. The different Mx2 variants are shown. The numbers of the amino acid residues at the boundaries of the domains are indicated. (B) SDS-PAGE of different His-Sumo-Mx2 constructs purified using Ni-NTA columns. The N-terminal 83-aa domain causes low levels of His-Sumo-(1-416) expression and solubility. (C) Gel-filtration profiles of different Mx2 constructs. The N-terminal His-Sumo-tags have been removed. ∆1-83, 84-416, and the stalk domain (417-680), mainly in the aggregation fraction; GF, only in the monomeric fraction. (D) Gel filtration profiles of His-Sumo-N-GF and N-GF. His-Sumo-N-GF and N-GF are mostly in the monomeric fraction. The Sumo-tag improved the stability of N-GF. A
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