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-Structure paper
タイトル | Impact of distinct FG nucleoporin repeats on Nup98 self-association. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 3797, Year 2024 |
掲載日 | 2024年5月7日 |
著者 | Alain Ibáñez de Opakua / Christian F Pantoja / Maria-Sol Cima-Omori / Christian Dienemann / Markus Zweckstetter / |
PubMed 要旨 | Nucleoporins rich in phenylalanine/glycine (FG) residues form the permeability barrier within the nuclear pore complex and are implicated in several pathological cellular processes, including ...Nucleoporins rich in phenylalanine/glycine (FG) residues form the permeability barrier within the nuclear pore complex and are implicated in several pathological cellular processes, including oncogenic fusion condensates. The self-association of FG-repeat proteins and interactions between FG-repeats play a critical role in these activities by forming hydrogel-like structures. Here we show that mutation of specific FG repeats of Nup98 can strongly decrease the protein's self-association capabilities. We further present a cryo-electron microscopy structure of a Nup98 peptide fibril with higher stability per residue compared with previous Nup98 fibril structures. The high-resolution structure reveals zipper-like hydrophobic patches which contain a GLFG motif and are less compatible for binding to nuclear transport receptors. The identified distinct molecular properties of different regions of the nucleoporin may contribute to spatial variations in the self-association of FG-repeats, potentially influencing transport processes through the nuclear pore. |
リンク | Nat Commun / PubMed:38714656 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.67 Å |
構造データ | EMDB-16671, PDB-8ci8: |
由来 |
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キーワード | PROTEIN FIBRIL / Nup98 / nuclear pore / FG repeats / amyloid fibrils |