 |
PDBsum entry 5b56
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Protein transport/viral protein
|
PDB id
|
|
|
|
5b56
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Molecular mechanism of HIV-1 vpr for binding to importin-α.
|
|
|
Authors
|
|
H.Miyatake,
A.Sanjoh,
T.Murakami,
H.Murakami,
G.Matsuda,
K.Hagiwara,
M.Yokoyama,
H.Sato,
Y.Miyamoto,
N.Dohmae,
Y.Aida.
|
|
|
Ref.
|
|
J Mol Biol, 2016,
428,
2744-2757.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Viral protein R (Vpr) is an accessory gene product of human immunodeficiency
virus type 1 (HIV-1) that plays multiple important roles associated with viral
replication. Structural studies using NMR have revealed that Vpr consists of
three α-helices and contains flexible N- and C-termini. However, the molecular
mechanisms associated with Vpr function have not been elucidated. To investigate
Vpr multifunctionality, we performed an X-ray crystallographic study of Vpr
complexes containing importin-α, a known Vpr binding partner present in host
cells. Elucidation of the crystal structure revealed that the flexible
C-terminus changes its conformation to a twisted β-turn via an induced-fit
mechanism, enabling binding to a minor nuclear localization signal (NLS) site of
importin-α. The Vpr C-terminus can also bind with major NLS sites of
importin-α in an extended conformation in different ways. These results, which
represent the first reported crystallographic analysis of Vpr, demonstrate the
multifunctional aspects that enable Vpr interaction with a variety of cellular
proteins.
|
|
|
|
|
|
|
