3NC0

Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II)

3NC0 の概要

• エントリーDOI: 10.2210/pdb3nc0/pdb
• 分子名称: Exportin-1, Snurportin-1, GTP-binding nuclear protein Ran, ... (9 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: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q6P5F9; Nucleus: O95149 P62826
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 373366.70

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 (2.9 Å)