 |
PDBsum entry 4jnu
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transport protein
|
PDB id
|
|
|
|
4jnu
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Architecture of the fungal nuclear pore inner ring complex.
|
|
|
Authors
|
|
T.Stuwe,
C.J.Bley,
K.Thierbach,
S.Petrovic,
S.Schilbach,
D.J.Mayo,
T.Perriches,
E.J.Rundlet,
Y.E.Jeon,
L.N.Collins,
F.M.Huber,
D.H.Lin,
M.Paduch,
A.Koide,
V.Lu,
J.Fischer,
E.Hurt,
S.Koide,
A.A.Kossiakoff,
A.Hoelz.
|
|
|
Ref.
|
|
Science, 2015,
350,
56-64.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional
nucleocytoplasmic transport. We present the reconstitution and interdisciplinary
analyses of the ~425-kilodalton inner ring complex (IRC), which forms the
central transport channel and diffusion barrier of the NPC, revealing its
interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57
channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the
adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96
functions as an assembly sensor that recognizes the three-dimensional
architecture of the CNT, thereby mediating the incorporation of a defined CNT
state into the NPC. We propose that the IRC adopts a relatively rigid scaffold
that recruits the CNT to primarily form the diffusion barrier of the NPC, rather
than enabling channel dilation.
|
|
|
|
|
|
|
