The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture
Name
Schwartz_The structure.pdf
Size
2.17 MB
Format
Adobe PDF
Checksum (MD5)
649698aa817f1182035fb0ae415d72a0
Author(s)
Leksa, Nina Carolina
Brohawn, Stephen G.
Schwartz, Thomas
Date Issued
July 2009
Journal
Structure
Publisher
Elsevier
Citation
Leksa, Nina C., Stephen G. Brohawn, and Thomas U. Schwartz. “The Structure of the Scaffold Nucleoporin Nup120 Reveals a New and Unexpected Domain Architecture.” Structure 17.8 (2009): 1082–1091.
Version
Author's final manuscript
Abstract
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous protein assemblies residing in circular openings in the nuclear envelope. The NPC is modular, with transient and stable components. The stable core is essentially built from two multiprotein complexes, the Y-shaped heptameric Nup84 complex and the Nic96 complex, arranged around an eightfold axis. We present the crystal structure of Nup120[subscript 1-757], one of the two short arms of the Y-shaped Nup84 complex. The protein adopts a compact oval shape built around a novel bipartite α-helical domain intimately integrated with a β-propeller domain. The domain arrangement is substantially different from the Nup85•Seh1 complex, which forms the other short arm of the Y. With the data presented here, we establish that all three branches of the Y-shaped Nup84 complex are tightly connected by helical interactions and that the β-propellers likely form interaction site(s) to neighboring complexes.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike 3.0
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.str.2009.06.003
