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Volume 32, No 5, May 2022

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 32 Issue 5, May 2022: 448-460   |  Open Access


Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex

Gaoxingyu Huang1,2,3,†,* , Xiechao Zhan1,2,3,† , Chao Zeng1,2,3,† , Ke Liang1,2,3,† , Xuechen Zhu1,2,3,† , Yanyu Zhao1,2,3 , Pan Wang4,5 , Qifan Wang1,2,3 , Qiang Zhou1,2,3 , Qinghua Tao4 , Minhao Liu4 , Jianlin Lei4 , Chuangye Yan4,5 , Yigong Shi1,2,3,4,5,*

1Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China
2Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China
3Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou, Zhejiang, China
4Beijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China
5Tsinghua University-Peking University Joint Center for Life Sciences; School of Life Sciences, Tsinghua University, Beijing, China
These authors contributed equally: Gaoxingyu Huang, Xiechao Zhan, Chao Zeng, Ke Liang, Xuechen Zhu
Correspondence: Gaoxingyu Huang( Shi(

Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from the Xenopus laevis NPC at an average resolution of 4.2 Å. A homo-dimer of Nup205 resides at the center of the IR subunit, flanked by two molecules of Nup188. Four molecules of Nup93 each places an extended helix into the axial groove of Nup205 or Nup188, together constituting the central scaffold. The channel nucleoporin hetero-trimer of Nup62/58/54 is anchored on the central scaffold. Six Nup155 molecules interact with the central scaffold and together with the NDC1–ALADIN hetero-dimers anchor the IR subunit to the nuclear envelope and to outer rings. The scarce inter-subunit contacts may allow sufficient latitude in conformation and diameter of the IR. Our structure reveals the molecular basis for the IR subunit assembly of a vertebrate NPC.


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