Simple fold composition and modular architecture of the nuclear pore complex

• DOI: 10.1073/pnas.0506345103
• Publication Date: 2006-02-07T01:33:05Z
• Authors: Damien Devos; Svetlana Dokudovs...; Rosemary Williams; Frank Alber; Narayanan Eswar; Brian T. Chait; Michael P. Rout; Andrej Sali
• Keywords: Nucleoporin; Nuclear pore

The nuclear pore complex (NPC) consists of multiple copies approximately 30 different proteins [nucleoporins (nups)], forming a channel in the envelope that mediates macromolecular transport between cytosol and nucleus. With <5% nup residues currently available experimentally determined structures, little is known about detailed structure NPC. Here, we use combined computational biochemical approach to assign folds for 95% yeast vertebrate nups. These fold assignments suggest an underlying simplicity composition modularity architecture all eukaryotic NPCs. NPC reflected presence only eight types, with three most frequent accounting 85% residues. its hierarchical symmetrical organization partitions predicted into groups: transmembrane group containing helices cadherin fold, central scaffold beta-propeller alpha-solenoid folds, peripheral FG predominantly repeats coiled-coil fold. Moreover, similarities structures coated vesicles those support our prior hypothesis their common evolutionary origin progenitor protocoatomer. small number types internal symmetries bulk has evolved through extensive motif gene duplication from simple precursor set few proteins.