1O6O

Importin Beta aa1-442 bound to five FxFG repeats from yeast Nsp1p. Second crystal form

1O6O の概要

• エントリーDOI: 10.2210/pdb1o6o/pdb
• 関連するPDBエントリー: 1F59 1IBR 1O6P 1QGK 1QGR
• 分子名称: IMPORTIN BETA-1 SUBUNIT, NUCLEOPORIN NSP1 (3 entities in total)
• 機能のキーワード: nuclear transport, nuclear trafficking, nucleoporin, transport factor, protein transport
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm: Q14974
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 185816.49

構造登録者

Bayliss, R.,Stewart, M. (登録日: 2002-10-10, 公開日: 2003-10-17, 最終更新日: 2023-12-13)

主引用文献

Bayliss, R.,Littlewood, T.,Strawn, L.A.,Wente, S.R.,Stewart, M.
Glfg and Fxfg Nucleoporins Bind to Overlapping Sites on Importin-Beta
J.Biol.Chem., 277:50597-, 2002

PubMed Abstract: The interaction between nuclear pore proteins (nucleoporins) and transport factors is crucial for the translocation of macromolecules through nuclear pores. Many nucleoporins contain FG sequence repeats, and previous studies have demonstrated interactions between repeats containing FxFG or GLFG cores and transport factors. The crystal structure of residues 1-442 of importin-beta bound to a GLFG peptide indicates that this repeat core binds to the same primary site as FxFG cores. Importin-beta-I178D shows reduced binding to both FxFG and GLFG repeats, consistent with both binding to an overlapping site in the hydrophobic groove between the A-helices of HEAT repeats 5 and 6. Moreover, FxFG repeats can displace importin-beta or its S. cerevisiae homologue, Kap95, bound to GLFG repeats. Addition of soluble GLFG repeats decreases the rate of nuclear protein import in digitonin-permeabilized HeLa cells, indicating that this interaction has a role in the translocation of carrier-cargo complexes through nuclear pores. The binding of GLFG and FxFG repeats to overlapping sites on importin-beta indicates that functional differences between different repeats probably arise from differences in their spatial organization.

PubMed: 12372823
DOI: 10.1074/JBC.M209037200

実験手法

X-RAY DIFFRACTION (2.8 Å)