The nuclear pore complex (NPC) serves as the sole bidirectional gateway of macromolecules in and out of the nucleus. Owing to its size and complexity (∼1,000 protein subunits, ∼110 MDa in humans), the NPC has remained one of the foremost challenges for structure determination. Structural studies have now provided atomic-resolution crystal structures of most nucleoporins. The acquisition of these structures, combined with biochemical reconstitution experiments, cross-linking mass spectrometry, and cryo-electron tomography, has facilitated the determination of the near-atomic overall architecture of the symmetric core of the human, fungal, and algal NPCs. Here, we discuss the insights gained from these new advances and outstanding issues regarding NPC structure and function. The powerful combination of bottom-up and top-down approaches toward determining the structure of the NPC offers a paradigm for uncovering the architectures of other complex biological machines to near-atomic resolution.

中文翻译：

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核孔复合体的结构（更新）。

核孔复合物（NPC）充当大分子进出核的唯一双向通道。由于其大小和复杂性（人体内约有1,000个蛋白质亚基，人中约有110个MDa），NPC仍然是确定结构的首要挑战之一。结构研究现已提供了大多数核孔蛋白的原子分辨晶体结构。这些结构的获取，再加上生化重建实验，交联质谱和冷冻电子断层扫描，已经促进了人类，真菌和藻类NPC对称核的近原子整体结构的确定。在这里，我们将讨论从这些新进展和有关NPC结构和功能的突出问题中获得的见解。