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Cryo-EM structure of full-length Nup188Cryo-EM structure of full-length Nup188
Structural highlights
Function[NU188_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization.[1] Publication Abstract from PubMedNuclear pore complexes (NPCs) mediate bidirectional nucleocytoplasmic transport of substances in eukaryotic cells. However, the accurate molecular arrangement of NPCs remains enigmatic owing to their huge size and highly dynamic nature. Here we determined the structure of the asymmetric unit of the inner ring (IR monomer) at 3.73 A resolution by single-particle cryo-electron microscopy, and created an atomic model of the intact IR consisting of 192 molecules of 8 nucleoporins. In each IR monomer, the Z-shaped Nup188-Nup192 complex in the middle layer is sandwiched by two approximately parallel rhomboidal structures in the inner and outer layers, while Nup188, Nup192 and Nic96 link all subunits to constitute a relatively stable IR monomer. In contrast, the intact IR is assembled by loose and instable interactions between IR monomers. These structures, together with previously reported structural information of IR, reveal two distinct interaction modes between IR monomers and extensive flexible connections in IR assembly, providing a structural basis for the stability and malleability of IR. Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.,Li Z, Chen S, Zhao L, Huang G, Pi X, Sun S, Wang P, Sui SF Cell Res. 2022 Mar 18. pii: 10.1038/s41422-022-00632-y. doi:, 10.1038/s41422-022-00632-y. PMID:35301440[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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