The nuclear pore complex (NPC) is a giant protein assembly that penetrates the double layers of the nuclear membrane. The overall structure of the NPC has approximately eightfold symmetry and is formed by approximately 30 nucleoporins. The great size and complexity of the NPC have hindered the study of its structure for many years until recent breakthroughs were achieved by integrating the latest high-resolution cryo-electron microscopy (cryo-EM), the emerging artificial intelligence-based modeling and all other available structural information from crystallography and mass spectrometry. Here, we review our latest knowledge of the NPC architecture and the history of its structural study from in vitro to in situ with progressively improved resolutions by cryo-EM, with a particular focus on the latest subnanometer-resolution structural studies. The future directions for structural studies of NPCs are also discussed.
International Workshop of 3D Molecular Imaging by Cryo-Electron Microscopy, Third K. H. Kuo Summer School of Electron Microscopy and Crystallography in 2010.
International Workshop of Advanced Image Processing of Cryo-Electron Microscopy, 2013
Get acquainted with Cryo-Electron Microscopy: First Chinese Workshop for Structural Biologists, 2015
International Workshop of Advanced Image Processing of Cryo-Electron Microscopy, 2015
Instutions
Instutions
Institute of Biophysics, Chinese Academy of Sciences
The Scripps Research Institute
Max Planck Institute of Biochemistry
Database
Database
National Center for Biotechnology Information(NCBI)
Protein Data Bank
The Electron Microscopy Data Bank
ExPASy Proteomics Server
Pfam
3D EM
3DEM
Tools and Softwars
Tools and Softwars
CCP4
CCP-EM
MOLE 2.0 (characterization of channels and pores in protein complex)
