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Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1

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Abstract

The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four α-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.

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Figure 1: Characterization of TapC and point mutants.
Figure 2: Solution structure of the Tap C-terminal domain.
Figure 3: Features of the Tap C-terminal domain.
Figure 4: Interaction between TapC and FG-nucleoporins.

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Acknowledgements

We are grateful to our colleagues in Cambridge and Heidelberg, especially R. Bayliss, T. Littlewood, K. Strässer and A. Weeds for their helpful comments and criticisms. We thank J.C. Yang for help in recording NMR spectra, S. Peak-Chew for N-terminal sequencing and mass spectroscopy, and G. Wong for preparing proteins. Supported in part by the Human Frontiers Science Program.

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Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    Richard P. Grant, David Neuhaus & Murray Stewart

  2. Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, Heidelberg, 69120, Germany

    Ed Hurt

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  1. Richard P. Grant
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Correspondence to Murray Stewart.

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Grant, R., Hurt, E., Neuhaus, D. et al. Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. Nat Struct Mol Biol 9, 247–251 (2002). https://doi.org/10.1038/nsb773

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