Structure of a trimeric nucleoporin complex reveals alternate oligomerization states

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 106; no. 42; pp. 17693 - 17698
• Main Authors: Nagy, Vivien, Hsia, Kuo-Chiang, Debler, Erik W, Kampmann, Martin, Davenport, Andrew M, Blobel, Günter, Hoelz, André
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 20.10.2009; National Acad Sciences
• Subjects: Architecture; Binding Sites; Binding, Competitive; Biochemistry; Biological Sciences; Cells; CRYSTAL STRUCTURE; Crystallography, X-Ray; ELECTRON MICROSCOPY; MATERIALS SCIENCE; Microscopy; Models, Molecular; Multiprotein Complexes - chemistry; Nuclear membrane; Nuclear pore; Nuclear Pore - chemistry; Nuclear pore complex proteins; Nuclear Pore Complex Proteins - chemistry; Promiscuity; Protein Interaction Domains and Motifs; Protein Structure, Quaternary; Proteins; RESOLUTION; Saccharomyces cerevisiae - chemistry; Saccharomyces cerevisiae Proteins - chemistry; SOLENOIDS; Yeasts

The heptameric Nup84 complex constitutes an evolutionarily conserved building block of the nuclear pore complex. Here, we present the crystal structure of the heterotrimeric Sec13·Nup145C·Nup84 complex, the centerpiece of the heptamer, at 3.2-Å resolution. Nup84 forms a U-shaped α-helical solenoid d...