• Corpus ID: 219573779

The nuclear pore complex as an entropic gate: theory and simulation

@article{Castellano2020TheNP,
  title={The nuclear pore complex as an entropic gate: theory and simulation},
  author={Mike Castellano and Steffen Wolf and Thorsten Koslowski},
  journal={arXiv: Biological Physics},
  year={2020}
}
Protein chains of the (FG)$_n$ ($n \simeq$ 300) type cap the cytoplasmatic side of the nucleopore complex, which connects the nucleus to the remainder of an eukaryotic cell. We study the properties of three fundamental polymer models that represent these filaments using Monte Carlo computer simulations. Random walks and the worm like chain model cannot account for the unusual size selectivity of the pore, while a two-dimensional arrangement of intrinsically disordered block copolymers with a… 

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References

SHOWING 1-10 OF 34 REFERENCES
Probing a structural model of the nuclear pore complex channel through molecular dynamics.
Structure and gating of the nuclear pore complex
TLDR
This work reconstructs the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 Å resolution by cryo-electron tomography in conjunction with subtomogram averaging and proposes a model for the architecture of the molecular gate at its central channel.
From the trap to the basket: getting to the bottom of the nuclear pore complex
TLDR
It is reexamine how NPCs can discriminate between receptor-mediated and passive cargo to promote vectorial translocation in a highly regulated manner and comment on the importance and potential benefits of identifying and experimenting with individual key components implicated in the translocation mechanism.
The nuclear pore complex – structure and function at a glance
TLDR
How transport between the nucleoplasm and the cytoplasm is regulated, what the authors currently know about the structure of individual nucleoporins and the assembled NPC, and how the cell regulates assembly and disassembly of such a massive structure are discussed.
Translocation Through the Nuclear Pore Complex: Selectivity and Speed by Reduction‐of‐Dimensionality
TLDR
It is suggested that nuclear transport receptors such as the karyopherins, in accordance with their peculiar boat‐like structure, act as nanoscopic ferries transporting cargos through the NPC by sliding on a surface of phenylalanine glycine (FG) motifs.
Molecular architecture of the inner ring scaffold of the human nuclear pore complex
TLDR
This architectural map explains the vast majority of the electron density of the scaffold, and concludes that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.
The Structure of the Nuclear Pore Complex (An Update).
TLDR
The powerful combination of bottom-up and top-down approaches toward determining the structure of the NPC offers a paradigm for uncovering the architectures of other complex biological machines to near-atomic resolution.
Cooperative Interactions between Different Classes of Disordered Proteins Play a Functional Role in the Nuclear Pore Complex of Baker’s Yeast
TLDR
Extension of the original DCBG model is extended by first performing coarse grained simulations of the single-block FG nups which confirm that they have a single block polymer structure rather than the di-block structure of tree nups, and molecular simulations demonstrate that these single-blocks are likely cohesive, compact, collapsed coil polymers.
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