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Cell Res June 1, 2020; 30 (6): 520-531.

Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.

Huang G , Zhang Y , Zhu X , Zeng C , Wang Q , Zhou Q , Tao Q , Liu M , Lei J , Yan C , Shi Y .

The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 Å for the cytoplasmic ring (CR). Here we present a single-particle cryo-electron microscopy (cryo-EM) structure of the CR from Xenopus laevis NPC at average resolutions of 5.5-7.9 Å, with local resolutions reaching 4.5 Å. Improved resolutions allow identification and placement of secondary structural elements in the majority of the CR components. The two Y complexes in each CR subunit interact with each other and associate with those from flanking subunits, forming a circular scaffold. Within each CR subunit, the Nup358-containing region wraps around the stems of both Y complexes, likely stabilizing the scaffold. Nup205 connects the short arms of the two Y complexes and associates with the stem of a neighboring Y complex. The Nup214-containing region uses an extended coiled-coil to link Nup85 of the two Y complexes and protrudes into the axial pore of the NPC. These previously uncharacterized structural features reveal insights into NPC assembly.

PubMed ID: 32376910
PMC ID: PMC7264146
Article link: Cell Res
Grant support: [+]
Genes referenced: kidins220 nup107 nup133 nup160 nup188 nup205 nup214 nup37 nup43 nup62 nup85 nup88 nup98 psmd6 ranbp2 sec13 sult2a1 tdgf1.2
GO keywords: nuclear pore

Article Images: [+] show captions

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