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Published August 25, 2009 | Published + Supplemental Material
Journal Article Open

Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex


The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a β propeller and an α-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC.

Additional Information

© 2009 National Academy of Sciences. Contributed by Günter Blobel, July 7, 2009 (received for review June 4, 2009). We thank K.-C. Hsia, V. Nagy, A. Patke, and P. Stavropoulos for discussions and comments on the manuscript; S. Etherton for help with editing the manuscript; D. King for mass spectrometry analysis; T. Huber for help with CD spectroscopy; V. Nagy for providing material; and A. Davenport for technical assistance. Analytical ultracentrifugation was carried out by the Wadsworth Center Biochemistry Core Facility; isothermal titration calorimetry by the Biophysics Core Facility at the University of Colorado Denver. We also thank W. Shi (NSLS) and M. Becker and R. Fischetti (GM/CA-CAT) 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). D.W. was supported by a fellowship of the German Academic Exchange Service. A.H. was supported by a grant from the Leukemia and Lymphoma Society. Author contributions: H.-S.S., Y.M., E.W.D., D.W., S.K., and A.H. designed research; H.-S.S., Y.M., E.W.D., D.W., S.K., and A.H. performed research; H.-S.S., Y.M., E.W.D., D.W., S.K., G.B., and A.H. analyzed data; and H.-S.S., E.W.D., and A.H. wrote the paper. The authors declare no conflict of interest. Data deposition: The atomic coordinates have been deposited in the Protein Data Bank, www.pdb.org (PDB ID codes 3F7F and 3H7N). This article contains supporting information online at www.pnas.org/cgi/content/full/0907453106/DCSupplemental.

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Published - 14281.full.pdf

Supplemental Material - 0907453106SI.pdf

Supplemental Material - SM1.mov

Supplemental Material - SM2.mov


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August 21, 2023
October 20, 2023