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

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 alpha-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.

Pubmed ID: 11875519

Authors

  • Grant RP
  • Hurt E
  • Neuhaus D
  • Stewart M

Journal

Nature structural biology

Publication Data

April 26, 2002

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Circular Dichroism
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA-Binding Proteins
  • Repetitive Sequences, Amino Acid
  • Sequence Alignment
  • Structure-Activity Relationship