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The Structure of the Nuclear Pore Complex (An Update).
Lin, Daniel H; Hoelz, André.
Afiliación
  • Lin DH; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA; email: hoelz@caltech.edu.
  • Hoelz A; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA; email: hoelz@caltech.edu.
Annu Rev Biochem ; 88: 725-783, 2019 06 20.
Article en En | MEDLINE | ID: mdl-30883195
The nuclear pore complex (NPC) serves as the sole bidirectional gateway of macromolecules in and out of the nucleus. Owing to its size and complexity (∼1,000 protein subunits, ∼110 MDa in humans), the NPC has remained one of the foremost challenges for structure determination. Structural studies have now provided atomic-resolution crystal structures of most nucleoporins. The acquisition of these structures, combined with biochemical reconstitution experiments, cross-linking mass spectrometry, and cryo-electron tomography, has facilitated the determination of the near-atomic overall architecture of the symmetric core of the human, fungal, and algal NPCs. Here, we discuss the insights gained from these new advances and outstanding issues regarding NPC structure and function. The powerful combination of bottom-up and top-down approaches toward determining the structure of the NPC offers a paradigm for uncovering the architectures of other complex biological machines to near-atomic resolution.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Modelos Moleculares / Poro Nuclear / Proteínas de Complejo Poro Nuclear Límite: Animals / Humans Idioma: En Revista: Annu Rev Biochem Año: 2019 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Modelos Moleculares / Poro Nuclear / Proteínas de Complejo Poro Nuclear Límite: Animals / Humans Idioma: En Revista: Annu Rev Biochem Año: 2019 Tipo del documento: Article