Dynamics of nuclear pore complexes: A computational insight into macromolecular traffic regulation*

Eukaryotic cells rely on membrane-enclosed compartments to segregate vital biological functions. For example, the nucleus separates replication and transcription from translation in the cytoplasm. Facilitating macromolecular traffic between these compartments are nuclear pore complexes (NPCs) within the nuclear envelope. The human NPC, one of the largest protein complexes, consists of nucleoporins (NUPs) forming a robust scaffold for regulating nucleocytoplasmic traffic. Traditionally viewed as static structures, gaining atomic-level insight into NPC architecture remains an arduous challenge. Recent advancements, integrating innovative experimental techniques and AI-driven structure prediction, have improved the precision of the existing structural models for the NUPs forming the macromolecular pore complex. In this study, we employ a structure-based computational approach to build molecular simulations for the human NPC. Our focus is on investigating the dilation and constriction dynamics of NPCs, facilitating the movement of macromolecules. This research offers a more precise grasp of NPC function, which may enhance our understanding of macromolecule transport.