The nuclear pore complex (NPC) mediates the flow of substances between the nucleus and cytoplasm in eukaryotic cells.Here we report the cryo-electron tomography (cryo-ET) structure of the luminal ring (LR) of the NPC from Xenopus laevis oocyte.The observed key structural features of the LR are independently confirmed by single-particle cnyo-electron microscopy (cryo-EM) analysis.The LR comprises eight butterfly-shaped subunits,each containing two symmetric wings.Each wing consists of four elongated,tubular protomers.Within the LR subunit,the eight protomers form a Finger domain,which directly contacts the fusion between the inner and outer nuclear membranes and a Grid domain,which serves as a rigid base for the Finger domain.Two neighboring LR subunits interact with each other through the lateral edges of their wings to constitute a Bumper domain,which displays two major conformations and appears to cushion neighboring NPCs.Our study reveals previously unknown features of the LR and potentially explains the elastic property of the NPC.