• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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


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


Nature structural biology

Publication Data

April 26, 2002

Associated Grants


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