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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 391, Issue 7


Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex

Orit Peleg
  • Polymer Physics, Department of Materials, ETH Zurich, Wolfgang-Pauli-Strasse 10, CH-8093 Zurich, Switzerland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Roderick Y.H. Lim
  • Biozentrum and the Swiss Nanoscience Institute, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2010-05-19 | DOI: https://doi.org/10.1515/bc.2010.092


Several biological mechanisms involve proteins or proteinaceous components that are intrinsically disordered. A case in point pertains to the nuclear pore complex (NPC), which regulates molecular transport between the nucleus and the cytoplasm. NPC functionality is dependent on unfolded domains rich in Phe-Gly (FG) repeats (i.e., FG-domains) that collectively act to promote or hinder cargo translocation. To a large extent, our understanding of FG-domain behavior is limited to in vitro investigations given the difficulty to resolve them directly in the NPC. Nevertheless, recent findings indicate a collective convergence towards rationalizing FG-domain function. This review aims to glean further insight into this fascinating problem by taking an objective look at the boundary conditions and contextual details underpinning FG-domain behavior in the NPC. Here, we treat the FG-domains as being commensurate with polymeric chains to address ambiguities such as for instance, how FG-domains tethered to the central channel of the NPC would behave differently as compared with their free-floating counterparts in solution. By bringing such fundamental questions to the fore, this review seeks to illuminate the importance of how such parameters can hold influence over the structure-function relation of intrinsically disordered proteins in the NPC and beyond.

Keywords: FG-domains; hydrogel; intrinsically unstructured proteins; nanopore; natively unfolded proteins; nucleocytoplasmic transport; polymer brush

About the article

Corresponding author

Received: 2010-02-16

Accepted: 2010-04-26

Published Online: 2010-05-19

Published in Print: 2010-07-01

Citation Information: Biological Chemistry, Volume 391, Issue 7, Pages 719–730, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.092.

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