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5CWU

Crystal structure of Chaetomium thermophilum Nup188 TAIL domain

5CWU の概要
エントリーDOI10.2210/pdb5cwu/pdb
関連するPDBエントリー5CWS 5CWT 5CWV 5CWW
分子名称Nucleoporin NUP188, GLYCEROL (2 entities in total)
機能のキーワードnucleocytoplasmic transport, transport protein
由来する生物種Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
タンパク質・核酸の鎖数8
化学式量合計356164.26
構造登録者
主引用文献Stuwe, T.,Bley, C.J.,Thierbach, K.,Petrovic, S.,Schilbach, S.,Mayo, D.J.,Perriches, T.,Rundlet, E.J.,Jeon, Y.E.,Collins, L.N.,Huber, F.M.,Lin, D.H.,Paduch, M.,Koide, A.,Lu, V.,Fischer, J.,Hurt, E.,Koide, S.,Kossiakoff, A.A.,Hoelz, A.
Architecture of the fungal nuclear pore inner ring complex.
Science, 350:56-64, 2015
Cited by
PubMed Abstract: The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.
PubMed: 26316600
DOI: 10.1126/science.aac9176
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.35 Å)
構造検証レポート
Validation report summary of 5cwu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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