2Q5D

Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second crystal form

2Q5D の概要

• エントリーDOI: 10.2210/pdb2q5d/pdb
• 関連するPDBエントリー: 1QGK 1UKL 2P8Q
• 分子名称: Importin beta-1 subunit, Snurportin-1 (2 entities in total)
• 機能のキーワード: heat repeat, ibb-domain, importin, karyopherin, snurportin, protein transport
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q14974; Nucleus: O95149
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 204571.13

構造登録者

Mitrousis, G.,Cingolani, G. (登録日: 2007-05-31, 公開日: 2008-01-22, 最終更新日: 2023-08-30)

主引用文献

Mitrousis, G.,Olia, A.S.,Walker-Kopp, N.,Cingolani, G.
Molecular Basis for the Recognition of Snurportin 1 by Importin {beta}.
J.Biol.Chem., 283:7877-7884, 2008

PubMed Abstract: The nuclear import of uridine-rich ribonucleoproteins is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this study, we demonstrate that the sIBB domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65 and includes the previously identified importin alpha IBB (alphaIBB) region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB domain to confer a low nanomolar binding affinity for importin beta (K(d) approximately 2 nm) in an interaction that, in vitro, is displaced by RanGTP. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of uridine-rich ribonucleoproteins into the nucleus.

PubMed: 18187419
DOI: 10.1074/jbc.M709093200

実験手法

X-RAY DIFFRACTION (3.2 Å)