Nature 450, 695-701 (29 November 2007) | doi:10.1038/nature06405; Received 20 April 2007; Accepted 22 October 2007

The molecular architecture of the nuclear pore complex

Frank Alber1,4, Svetlana Dokudovskaya2,4,5, Liesbeth M. Veenhoff2,4,5, Wenzhu Zhang3, Julia Kipper2,5, Damien Devos1,5, Adisetyantari Suprapto2,5, Orit Karni-Schmidt2,5, Rosemary Williams2, Brian T. Chait3, Andrej Sali1 & Michael P. Rout2

  1. Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, Mission Bay QB3, 1700 4th Street, Suite 503B, University of California at San Francisco, San Francisco, California 94158-2330, USA
  2. Laboratory of Cellular and Structural Biology, and,
  3. Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA
  4. These authors contributed equally to this work.
  5. Present addresses: Laboratory of Nucleocytoplasmic Transport, Institut Jacques Monod, 2 place Jussieu, Tour 43, Paris 75251, France (S.D.); Department of Biochemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands (L.M.V.); German Aerospace Center (PT-DLR), Heinrich-Konen-Strasse 1, D-53227 Bonn, Germany (J.K.); Structural Bioinformatics, EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany (D.D.); Office of Technology Transfer, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA (A.S.); Herbert Irving Comprehensive Cancer Centre, Columbia University, 1130 St Nicholas Avenue, New York, New York 10032, USA (O.K.-S.).

Correspondence to: Brian T. Chait3Andrej Sali1Michael P. Rout2 Correspondence and requests for materials should be addressed to M.P.R (Email:, A.S. (Email:, or B.T.C. (Email:


Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50 MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPC's 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold. The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents, the most striking of these being a 16-fold repetition of 'columns'. These findings provide clues to the evolutionary origins of the NPC.


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