7CRU

hnRNPK NLS in complex with Importin alpha 1 (KPNA2)

7CRU の概要

• エントリーDOI: 10.2210/pdb7cru/pdb
• 分子名称: Heterogeneous nuclear ribonucleoprotein K, Importin subunit alpha-1, ACETATE ION, ... (5 entities in total)
• 機能のキーワード: importin alpha, hnrnpk, nls, complex, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 105182.08

構造登録者

Yao, J.,Sun, Q. (登録日: 2020-08-14, 公開日: 2021-11-17, 最終更新日: 2023-11-29)

主引用文献

Yao, J.,Tu, Y.,Shen, C.,Zhou, Q.,Xiao, H.,Jia, D.,Sun, Q.
Nuclear import receptors and hnRNPK mediates nuclear import and stress granule localization of SIRLOIN.
Cell.Mol.Life Sci., 78:7617-7633, 2021

PubMed Abstract: The majority of lncRNAs and a small fraction of mRNAs localize in the cell nucleus to exert their functions. A SIRLOIN RNA motif was previously reported to drive its nuclear localization by the RNA-binding protein hnRNPK. However, the underlying mechanism remains unclear. Here, we report crystal structures of hnRNPK in complex with SIRLOIN, and with the nuclear import receptor (NIR) Impα1, respectively. The protein hnRNPK bound to SIRLOIN with multiple weak interactions, and interacted Impα1 using an independent high-affinity site. Forming a complex with hnRNPK and Impα1 was essential for the nuclear import and stress granule localization of SIRLOIN in semi-permeabilized cells. Nuclear import of SIRLOIN enhanced with increasing NIR concentrations, but its stress granule localization peaked at a low NIR concentration. Collectively, we propose a mechanism of SIRLOIN localization, in which NIRs functioned as drivers/regulators, and hnRNPK as an adaptor.

PubMed: 34689235
DOI: 10.1007/s00018-021-03992-7

実験手法

X-RAY DIFFRACTION (2.8 Å)