3NBY

Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex

3NBY の概要

• エントリーDOI: 10.2210/pdb3nby/pdb
• 分子名称: Snurportin-1, GTP-binding nuclear protein Ran, Exportin-1, ... (5 entities in total)
• 機能のキーワード: protein transport, gtp-binding protein-transport protein complex, gtp-binding protein/transport protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm (By similarity): O95149; Nucleus: P62826 Q6P5F9
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 370671.65

構造登録者

Guttler, T.,Madl, T.,Neumann, P.,Deichsel, D.,Corsini, L.,Monecke, T.,Ficner, R.,Sattler, M.,Gorlich, D. (登録日: 2010-06-04, 公開日: 2010-10-27, 最終更新日: 2023-09-06)

主引用文献

Guttler, T.,Madl, T.,Neumann, P.,Deichsel, D.,Corsini, L.,Monecke, T.,Ficner, R.,Sattler, M.,Gorlich, D.
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1.
Nat.Struct.Mol.Biol., 17:1367-1376, 2010

PubMed Abstract: Classic nuclear export signals (NESs) confer CRM1-dependent nuclear export. Here we present crystal structures of the RanGTP-CRM1 complex alone and bound to the prototypic PKI or HIV-1 Rev NESs. These NESs differ markedly in the spacing of their key hydrophobic (Φ) residues, yet CRM1 recognizes them with the same rigid set of five Φ pockets. The different Φ spacings are compensated for by different conformations of the bound NESs: in the case of PKI, an α-helical conformation, and in the case of Rev, an extended conformation with a critical proline docking into a Φ pocket. NMR analyses of CRM1-bound and CRM1-free PKI NES suggest that CRM1 selects NES conformers that pre-exist in solution. Our data lead to a new structure-based NES consensus, and explain why NESs differ in their affinities for CRM1 and why supraphysiological NESs bind the exportin so tightly.

PubMed: 20972448
DOI: 10.1038/nsmb.1931

実験手法

X-RAY DIFFRACTION (3.42 Å)