3h7n
From Proteopedia
Structure of Nup120
Structural highlights
Function[NU120_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a beta propeller and an alpha-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC. Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex.,Seo HS, Ma Y, Debler EW, Wacker D, Kutik S, Blobel G, Hoelz A Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14281-6. Epub 2009 Aug 11. PMID:19706512[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Saccharomyces cerevisiae | Blobel, G | Debler, E W | Hoelz, A | Ma, Y | Seo, H S | Alpha-helical solenoid domain | Beta-propeller | Macromolecular assembly | Membrane | Membrane coat | Mrna transport | Nuclear pore complex | Nucleocytoplasmic transport | Nucleoporin | Nucleus | Phosphoprotein | Protein transport | Structural protein | Translocation | Transport
