Lingling Miao and Klaus Schulten.
Transport-related structures and processes of the nuclear pore
complex studied through molecular dynamics.
Structure, 17:449-459, 2009.
(PMC: 2701619)
MIAO2009
Nuclear pore complexes (NPCs) are selectively gated pathways between
nucleoplasm and cytoplasm. While small molecules can diffuse freely
through NPCs, large molecules (>40 kD) can pass only when bound to
transport receptors. The NPC central channel is filled with disordered
proteins, rich in phenylalanine-glycine (FG) repeats, referred to as
FG-nups. Our simulations, carried out at coarse-grained and all-atom
levels, show that arrays of FG-nups tethered to a planar surface, at
an FG-repeat density found in the NPC, form dynamic brush-like
structures of multi-protein bundles, while individual FG-nups form
dynamic globular structures. More than half of the FG-repeats are
found on the surface of the bundles, offering a favorable environment
for transport receptors. Binding to FG-repeats and a sliding motion of
NTF2 induced by binding and unbinding to phenylalanines were observed
when adding this transport receptor into one of the brush-like
structures.
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