The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture
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 he...
| Main Authors: | , , |
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| Format: | Article |
| Language: | en_US |
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Elsevier
2012
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| Online Access: | http://hdl.handle.net/1721.1/74556 https://orcid.org/0000-0001-8012-1512 |
| _version_ | 1811094317853310976 |
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| author | Leksa, Nina Carolina Brohawn, Stephen G. Schwartz, Thomas |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Leksa, Nina Carolina Brohawn, Stephen G. Schwartz, Thomas |
| author_sort | Leksa, Nina Carolina |
| collection | MIT |
| description | 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. |
| first_indexed | 2024-09-23T15:58:08Z |
| format | Article |
| id | mit-1721.1/74556 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T15:58:08Z |
| publishDate | 2012 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/745562022-10-02T05:24:21Z The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture Leksa, Nina Carolina Brohawn, Stephen G. Schwartz, Thomas Massachusetts Institute of Technology. Department of Biology Leksa, Nina Carolina Brohawn, Stephen G. Schwartz, Thomas U. 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. National Institutes of Health (U.S.) (Grant GM77537) Pew Charitable Trusts (Scholar Award) 2012-11-01T19:50:54Z 2012-11-01T19:50:54Z 2009-07 2009-06 Article http://purl.org/eprint/type/JournalArticle http://hdl.handle.net/1721.1/74556 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. https://orcid.org/0000-0001-8012-1512 en_US http://dx.doi.org/10.1016/j.str.2009.06.003 Structure Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Elsevier PMC |
| spellingShingle | Leksa, Nina Carolina Brohawn, Stephen G. Schwartz, Thomas The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title | The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title_full | The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title_fullStr | The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title_full_unstemmed | The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title_short | The structure of the scaffold nucleoporin Nup120 reveals a new and unexpected domain architecture |
| title_sort | structure of the scaffold nucleoporin nup120 reveals a new and unexpected domain architecture |
| url | http://hdl.handle.net/1721.1/74556 https://orcid.org/0000-0001-8012-1512 |
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