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Published October 20, 2009 | Published + Supplemental Material
Journal Article Open

Structure of a trimeric nucleoporin complex reveals alternate oligomerization states


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 domain, topologically similar to two other members of the heptamer, Nup145C and Nup85. The interaction between Nup84 and Nup145C is mediated via a hydrophobic interface located in the kink regions of the two solenoids that is reinforced by additional interactions of two long Nup84 loops. The Nup84 binding site partially overlaps with the homo-dimerization interface of Nup145C, suggesting competing binding events. Fitting of the elongated Z-shaped heterotrimer into electron microscopy (EM) envelopes of the heptamer indicates that structural changes occur at the Nup145C·Nup84 interface. Docking the crystal structures of all heptamer components into the EM envelope constitutes a major advance toward the completion of the structural characterization of the Nup84 complex.

Additional Information

© 2009 National Academy of Sciences. Contributed by Günter Blobel, August 19, 2009 (received for review July 6, 2009). We thank A. Patke, H.-S. Seo, and T. Strowig for discussions and comments on the manuscript; S. Etherton for help with editing the manuscript; D. King for mass spectrometry analysis; and S. Kuebler (Wyatt Technology) and S. Solmaz for assistance with the multiangle light scattering analysis. Edman sequencing was carried out by J. Fernandez at the Rockefeller University Proteomics Resource Center. Analytical ultracentrifugation and isothermal titration calorimetry were carried out by L. Eisele at the Wadsworth Center Biochemistry Core Facility and by S. Bevers at the Biophysics Core Facility at the University of Colorado Denver, respectively. In addition, we thank M. Becker, R. Sanishvili, and R. Fischetti (APS); J. Dickert, S. Morton, K. Royal, and C. Ralston (ALS); and W. Shi (NSLS), for support during data collection. E.W.D. is the Dale F. and Betty Ann Frey Fellow of the Damon Runyon Cancer Research Foundation (DRG-1977-08). A.H. was supported by a grant from the Leukemia and Lymphoma Society. Author contributions: V.N. and A.H. designed research; V.N., K.-C.H., E.W.D., A.M.D., and A.H. performed research; V.N., K.-C.H., E.W.D., M.K., G.B., and A.H. analyzed data; and V.N., E.W.D., G.B., and A.H. wrote the paper. The authors declare no conflict of interest. Data deposition: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 3IKO). This article contains supporting information online at www.pnas.org/cgi/content/full/0909373106/DCSupplemental.

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Supplemental Material - 0909373106SI.pdf

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August 21, 2023
October 20, 2023