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-Structure paper
タイトル | Integrated structural analysis of the human nuclear pore complex scaffold. |
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ジャーナル・号・ページ | Cell, Vol. 155, Issue 6, Page 1233-1243, Year 2013 |
掲載日 | 2013年12月5日 |
著者 | Khanh Huy Bui / Alexander von Appen / Amanda L DiGuilio / Alessandro Ori / Lenore Sparks / Marie-Therese Mackmull / Thomas Bock / Wim Hagen / Amparo Andrés-Pons / Joseph S Glavy / Martin Beck / |
PubMed 要旨 | The nuclear pore complex (NPC) is a fundamental component of all eukaryotic cells that facilitates nucleocytoplasmic exchange of macromolecules. It is assembled from multiple copies of about 30 ...The nuclear pore complex (NPC) is a fundamental component of all eukaryotic cells that facilitates nucleocytoplasmic exchange of macromolecules. It is assembled from multiple copies of about 30 nucleoporins. Due to its size and complex composition, determining the structure of the NPC is an enormous challenge, and the overall architecture of the NPC scaffold remains elusive. In this study, we have used an integrated approach based on electron tomography, single-particle electron microscopy, and crosslinking mass spectrometry to determine the structure of a major scaffold motif of the human NPC, the Nup107 subcomplex, in both isolation and integrated into the NPC. We show that 32 copies of the Nup107 subcomplex assemble into two reticulated rings, one each at the cytoplasmic and nuclear face of the NPC. This arrangement may explain how changes of the diameter are realized that would accommodate transport of huge cargoes. |
リンク | Cell / PubMed:24315095 |
手法 | EM (サブトモグラム平均) |
解像度 | 34.0 - 39.0 Å |
構造データ | EMDB-2443: EMDB-2444: EMDB-2445: |
由来 |
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