1UN0

Crystal Structure of Yeast Karyopherin (Importin) alpha in complex with a Nup2p N-terminal fragment

1UN0 の概要

• エントリーDOI: 10.2210/pdb1un0/pdb
• 関連するPDBエントリー: 1BK5 1BK6 1EE4 1EE5
• 分子名称: IMPORTIN ALPHA SUBUNIT, NUCLEOPORIN NUP2 (3 entities in total)
• 機能のキーワード: nuclear import, armadillo repeat, nucleoporin, nls release, karyopherin recycling
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm, perinuclear region: Q02821; Nucleus, nuclear pore complex: P32499
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 109440.42

構造登録者

Matsuura, Y.,Lange, A.,Harreman, M.T.,Corbett, A.H.,Stewart, M. (登録日: 2003-09-03, 公開日: 2003-10-16, 最終更新日: 2023-12-13)

主引用文献

Matsuura, Y.,Lange, A.,Harreman, M.T.,Corbett, A.H.,Stewart, M.
Structural Basis for Nup2P Function in Cargo Release and Karyopherin Recycling in Nuclear Import
Embo J., 22:5358-, 2003

PubMed Abstract: The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of nuclear pore complexes and is required for efficient importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p and are required for Nup2p function in vivo. We have determined the 2.6 A resolution crystal structure of a complex between this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of Kap60p, but its interaction interface is different from that employed for nuclear localization signal (NLS) recognition although there is some overlap between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the presence of the importin-beta binding (IBB) domain of Kap60p. These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process.

PubMed: 14532109
DOI: 10.1093/EMBOJ/CDG538

実験手法

X-RAY DIFFRACTION (2.6 Å)