7PER
Model of the inner ring of the human nuclear pore complex
Summary for 7PER
Entry DOI | 10.2210/pdb7per/pdb |
EMDB information | 12814 |
Descriptor | Nucleoporin p54, Nucleoporin p58/p45, Nuclear pore glycoprotein p62, ... (6 entities in total) |
Functional Keywords | nuclear pore complex, npc, transport protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 24 |
Total formula weight | 2587405.87 |
Authors | Schuller, A.P.,Wojtynek, M.,Mankus, D.,Tatli, M.,Kronenberg-Tenga, R.,Regmi, S.G.,Dasso, M.,Weis, K.,Medalia, O.,Schwartz, T.U. (deposition date: 2021-08-11, release date: 2021-10-20, Last modification date: 2024-10-16) |
Primary citation | Schuller, A.P.,Wojtynek, M.,Mankus, D.,Tatli, M.,Kronenberg-Tenga, R.,Regmi, S.G.,Dip, P.V.,Lytton-Jean, A.K.R.,Brignole, E.J.,Dasso, M.,Weis, K.,Medalia, O.,Schwartz, T.U. The cellular environment shapes the nuclear pore complex architecture. Nature, 598:667-671, 2021 Cited by PubMed Abstract: Nuclear pore complexes (NPCs) create large conduits for cargo transport between the nucleus and cytoplasm across the nuclear envelope (NE). These multi-megadalton structures are composed of about thirty different nucleoporins that are distributed in three main substructures (the inner, cytoplasmic and nucleoplasmic rings) around the central transport channel. Here we use cryo-electron tomography on DLD-1 cells that were prepared using cryo-focused-ion-beam milling to generate a structural model for the human NPC in its native environment. We show that-compared with previous human NPC models obtained from purified NEs-the inner ring in our model is substantially wider; the volume of the central channel is increased by 75% and the nucleoplasmic and cytoplasmic rings are reorganized. Moreover, the NPC membrane exhibits asymmetry around the inner-ring complex. Using targeted degradation of Nup96, a scaffold nucleoporin of the cytoplasmic and nucleoplasmic rings, we observe the interdependence of each ring in modulating the central channel and maintaining membrane asymmetry. Our findings highlight the inherent flexibility of the NPC and suggest that the cellular environment has a considerable influence on NPC dimensions and architecture. PubMed: 34646014DOI: 10.1038/s41586-021-03985-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (35 Å) |
Structure validation
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