3ZIR

minor-site specific NLS (B141)

3ZIR の概要

• エントリーDOI: 10.2210/pdb3zir/pdb
• 関連するPDBエントリー: 3ZIN 3ZIO 3ZIP 3ZIQ
• 分子名称: IMPORTIN SUBUNIT ALPHA-2, B141NLS (3 entities in total)
• 機能のキーワード: transport protein, nuclear import, nuclear localization signals
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P52293
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 52866.31

構造登録者

Chang, C.-W.,Counago, R.M.,Williams, S.J.,Kobe, B. (登録日: 2013-01-10, 公開日: 2013-08-21, 最終更新日: 2023-12-20)

主引用文献

Chang, C.-W.,Counago, R.M.,Williams, S.J.,Boden, M.,Kobe, B.
Distinctive Conformation of Minor Site-Specific Nuclear Localization Signals Bound to Importin-Alpha
Traffic, 14:1144-, 2013

PubMed Abstract: Nuclear localization signals (NLSs) contain one or two clusters of basic residues and are recognized by the import receptor importin-α. There are two NLS-binding sites (major and minor) on importin-α and the major NLS-binding site is considered to be the primary binding site. Here, we used crystallographic and biochemical methods to investigate the binding between importin-α and predicted 'minor site-specific' NLSs: four peptide library-derived peptides, and the NLS from mouse RNA helicase II/Guα. The crystal structures reveal that these atypical NLSs indeed preferentially bind to the minor NLS-binding site. Unlike previously characterized NLSs, the C-terminal residues of these NLSs form an α-helical turn, stabilized by internal H-bond and cation-π interactions between the aromatic residues from the NLSs and the positively charged residues from importin-α. This helical turn sterically hinders binding at the major NLS-binding site, explaining the minor-site preference. Our data suggest the sequence RXXKR[K/X][F/Y/W]XXAF as the optimal minor NLS-binding site-specific motif, which may help identify novel proteins with atypical NLSs.

PubMed: 23910026
DOI: 10.1111/TRA.12098

実験手法

X-RAY DIFFRACTION (2.3 Å)