The only bidirectional entry and exit point for macromolecules into and out of the nucleus is the nuclear pore complex (NPC). The NPC has remained one of the biggest problems for structure determination because of its size and complexity (1,000 protein subunits, 110 MDa in humans). The majority of nucleoporins now have atomic-resolution crystal structures thanks to structural research. With the help of biochemical reconstitution experiments, cross-linking mass spectrometry, and cryo-electron tomography, the acquisition of these structures has made it easier to determine the near-atomic overall architecture of the symmetric core of the human, fungus, and algal NPCs (Elmlinger MW et al., 2002). Here, we go over the knowledge obtained from these recent developments and unresolved problems with relation to NPC form and operation. The potent combination of top-down and bottom-up methods used to determine the NPC's structure provides a framework for identifying the architectures of other complex biological machines with almost atomic precision (Elmlinger MW et al., 2005).
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