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  A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.

Zahn, R., Osmanovic, D., Ehret, S., Callis, C. A., Frey, S., Stewart, M., et al. (2016). A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies. eLife, 5: e14119. doi:10.7554/eLife.14119.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-EE01-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2E47-6
Genre: Journal Article

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 Creators:
Zahn, R., Author
Osmanovic, D., Author
Ehret, S., Author
Callis, C. A., Author
Frey, S.1, Author              
Stewart, M., Author
You, C. J., Author
Görlich, D.1, Author              
Hoogenboom, B. W., Author
Richter, R. P., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              

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 Abstract: The permeability barrier of nuclear pore complexes (NPCs) controls bulk nucleocytoplasmic exchange. It consists of nucleoporin domains rich in phenylalanine-glycine motifs (FG domains). As a bottom-up nanoscale model for the permeability barrier, we have used planar films produced with three different end-grafted FG domains, and quantitatively analyzed the binding of two different nuclear transport receptors (NTRs), NTF2 and Importin beta, together with the concomitant film thickness changes. NTR binding caused only moderate changes in film thickness; the binding isotherms showed negative cooperativity and could all be mapped onto a single master curve. This universal NTR binding behavior a key element for the transport selectivity of the NPC was quantitatively reproduced by a physical model that treats FG domains as regular, flexible polymers, and NTRs as spherical colloids with a homogeneous surface, ignoring the detailed arrangement of interaction sites along FG domains and on the NTR surface.

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Language(s): eng - English
 Dates: 2016-04-08
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.14119
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Title: eLife
Source Genre: Journal
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Pages: 21 Volume / Issue: 5 Sequence Number: e14119 Start / End Page: - Identifier: -