3UL1

Mouse importin alpha: nucleoplasmin cNLS peptide complex

3UL1 の概要

• エントリーDOI: 10.2210/pdb3ul1/pdb
• 関連するPDBエントリー: 1EE5 1EJY 1IAL 3UKW 3UKX 3UKY 3UKZ 3UL0
• 分子名称: Importin subunit alpha-2, Nucleoplasmin (3 entities in total)
• 機能のキーワード: arm repeat, armadillo repeat, nuclear transport, nuclear localisation signal binding, importin beta binding, protein transport-nuclear protein complex, protein transport/nuclear protein
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P52293; Nucleus: P05221
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57558.24

構造登録者

Marfori, M.,Forwood, J.K.,Lonhienne, T.G.,Kobe, B. (登録日: 2011-11-10, 公開日: 2012-10-03, 最終更新日: 2023-11-01)

主引用文献

Marfori, M.,Lonhienne, T.G.,Forwood, J.K.,Kobe, B.
Structural Basis of High-Affinity Nuclear Localization Signal Interactions with Importin-alpha
Traffic, 13:532-548, 2012

PubMed Abstract: Classical nuclear localization signals (cNLSs), comprising one (monopartite cNLSs) or two clusters of basic residues connected by a 10-12 residue linker (bipartite cNLSs), are recognized by the nuclear import factor importin-α. The cNLSs bind along a concave groove on importin-α; however, specificity determinants of cNLSs remain poorly understood. We present a structural and interaction analysis study of importin-α binding to both designed and naturally occurring high-affinity cNLS-like sequences; the peptide inhibitors Bimax1 and Bimax2, and cNLS peptides of cap-binding protein 80. Our data suggest that cNLSs and cNLS-like sequences can achieve high affinity through maximizing interactions at the importin-α minor site, and by taking advantage of multiple linker region interactions. Our study defines an extended set of binding cavities on the importin-α surface, and also expands on recent observations that longer linker sequences are allowed, and that long-range electrostatic complementarity can contribute to cNLS-binding affinity. Altogether, our study explains the molecular and structural basis of the results of a number of recent studies, including systematic mutagenesis and peptide library approaches, and provides an improved level of understanding on the specificity determinants of a cNLS. Our results have implications for identifying cNLSs in novel proteins.

PubMed: 22248489
DOI: 10.1111/j.1600-0854.2012.01329.x

実験手法

X-RAY DIFFRACTION (1.9 Å)