5UWP

Crystal Structure of mDia2 NES Peptide in complex with CRM1-Ran-RanBP1

5UWP の概要

• エントリーDOI: 10.2210/pdb5uwp/pdb
• 関連するPDBエントリー: 5UWH 5UWI 5UWJ 5UWO 5UWQ 5UWR 5UWS 5UWT 5UWU 5UWW
• 分子名称: GTP-binding nuclear protein Ran, Ran-specific GTPase-activating protein 1, Exportin-1, ... (8 entities in total)
• 機能のキーワード: heat repeat, nes, nuclear export, karyopherin, protein transport
• 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: 163565.30

構造登録者

Fung, H.Y.J.,Chook, Y.M. (登録日: 2017-02-21, 公開日: 2017-03-22, 最終更新日: 2024-03-06)

主引用文献

Fung, H.Y.,Fu, S.C.,Chook, Y.M.
Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals.
Elife, 6:-, 2017

PubMed Abstract: Nuclear export receptor CRM1 binds highly variable nuclear export signals (NESs) in hundreds of different cargoes. Previously we have shown that CRM1 binds NESs in both polypeptide orientations (Fung et al., 2015). Here, we show crystal structures of CRM1 bound to eight additional NESs which reveal diverse conformations that range from loop-like to all-helix, which occupy different extents of the invariant NES-binding groove. Analysis of all NES structures show 5-6 distinct backbone conformations where the only conserved secondary structural element is one turn of helix that binds the central portion of the CRM1 groove. All NESs also participate in main chain hydrogen bonding with human CRM1 Lys568 side chain, which acts as a specificity filter that prevents binding of non-NES peptides. The large conformational range of NES backbones explains the lack of a fixed pattern for its 3-5 hydrophobic anchor residues, which in turn explains the large array of peptide sequences that can function as NESs.

PubMed: 28282025
DOI: 10.7554/eLife.23961

実験手法

X-RAY DIFFRACTION (2.054 Å)