title: The structure of the nuclear pore complex.
abstract: In eukaryotic cells, the spatial segregation of replication and transcription in the nucleus and translation in the cytoplasm imposes the requirement of transporting thousands of macromolecules between these two compartments. Nuclear pore complexes (NPCs) are the sole gateways that facilitate this macromolecular exchange across the nuclear envelope with the help of soluble transport receptors. Whereas the mobile transport machinery is reasonably well understood at the atomic level, a commensurate structural characterization of the NPC has only begun in the past few years. Here, we describe the recent progress toward the elucidation of the atomic structure of the NPC, highlight emerging concepts of its underlying architecture, and discuss key outstanding questions and challenges. The applied structure determination as well as the described design principles of the NPC may serve as paradigms for other macromolecular assemblies.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA. hoelz@caltech.edu
authors.forename: André
authors.initials: A
authors.lastname: Hoelz
authors.forename: Erik W
authors.initials: EW
authors.lastname: Debler
authors.forename: Günter
authors.initials: G
authors.lastname: Blobel
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D009685:Nuclear Envelope / Q000737:chemistry / Q000378:metabolism; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D028961:beta Karyopherins / Q000737:chemistry / Q000378:metabolism
chemical_list: D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D028961:beta Karyopherins