ArticleBiophysical journal2010
Hydrophilic linkers and polar contacts affect aggregation of FG repeat peptides.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Thermodynamic Compensation in Peptides Following Liquid-Liquid Phase Separation.The journal of physical chemistry. B · 2021Article
- Poor old pores-The challenge of making and maintaining nuclear pore complexes in aging.The FEBS journal · 2020Review
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
- Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex.Scientific reports · 2015Article
- Assembly of Nsp1 nucleoporins provides insight into nuclear pore complex gating.PLoS computational biology · 2014Article
- Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153.Biophysical journal · 2011Article
- Brownian dynamics simulation of nucleocytoplasmic transport: a coarse-grained model for the functional state of the nuclear pore complex.PLoS computational biology · 2011Article
- Interaction of β-sheet folds with a gold surface.PloS one · 2011Article
- How sequence determines elasticity of disordered proteins.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transport of large proteins into the nucleus involves two events, binding of the cargo protein to a transport receptor in the cytoplasm and passage of the cargo-transporter complex through the selective permeability barrier of the nuclear pore complex. The permeability barrier is formed by largely disordered polypeptides, each containing a number of conserved hydrophobic phenylalanine-glycine (FG) sequence motifs, connected by hydrophilic linkers of varying sequence (FG nups). How the motifs interact to form the permeability barrier, however, is not yet known. We have, therefore, carried out molecular dynamics simulations on various model FG repeat peptides to study the aggregation propensity of FG nups and the specific roles of the hydrophobic FG motifs and the hydrophilic linkers. Our simulations show spontaneous aggregation of the model nups into hydrated aggregates, which exhibit structural features assumed to be part of the permeability barrier. Our simulations suggest that short beta-sheets are an important structural feature of the aggregates and that Phe residues are sufficiently exposed to allow rapid binding of transport receptors. A surprisingly large influence of the amino acid composition of the hydrophilic linkers on aggregation is seen, as well as a major contribution of hydrogen-bonding patterns.
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