5DIS

Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid FG-repeat containing fragment of Nup214

5DIS の概要

• エントリーDOI: 10.2210/pdb5dis/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Exportin-1, GTP-binding nuclear protein Ran, Snurportin-1, ... (9 entities in total)
• 機能のキーワード: fg-repeats, nucleoporin, nup214, exportin, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 225181.86

構造登録者

Monecke, T.,Port, S.A.,Dickmanns, A.,Kehlenbach, R.H.,Ficner, R. (登録日: 2015-09-01, 公開日: 2015-11-04, 最終更新日: 2024-01-10)

主引用文献

Port, S.A.,Monecke, T.,Dickmanns, A.,Spillner, C.,Hofele, R.,Urlaub, H.,Ficner, R.,Kehlenbach, R.H.
Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export.
Cell Rep, 13:690-702, 2015

PubMed Abstract: CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 Å resolution. The structure reveals eight binding sites for Nup214 FG motifs on CRM1, with intervening stretches that are loosely attached to the transport receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping CRM1 in a closed conformation and stabilizing the export complex. The role of conserved hydrophobic pockets for the recognition of FG motifs was analyzed in biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions.

PubMed: 26489467
DOI: 10.1016/j.celrep.2015.09.042

実験手法

X-RAY DIFFRACTION (2.85 Å)