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Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.

TAP-p15 heterodimers have been implicated in the export of mRNAs through nuclear pore complexes (NPCs). We report a structural analysis of the interaction domains of TAP and p15 in a ternary complex with a Phe-Gly (FG) repeat of an NPC component. The TAP-p15 heterodimer is structurally similar to the homodimeric transport factor NTF2, but unlike NTF2, it is incompatible with either homodimerization or Ran binding. The NTF2-like heterodimer functions as a single structural unit in recognizing an FG repeat at a hydrophobic pocket present only on TAP and not on p15. This FG binding site interacts synergistically with a second site at the C terminus of TAP to mediate mRNA transport through the pore. In general, our findings suggest that FG repeats bind with a similar conformation to different classes of transport factors.

Pubmed ID: 11583626


  • Fribourg S
  • Braun IC
  • Izaurralde E
  • Conti E


Molecular cell

Publication Data

September 3, 2001

Associated Grants


Mesh Terms

  • ATP-Binding Cassette Transporters
  • Active Transport, Cell Nucleus
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Crystallography, X-Ray
  • Dimerization
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Nuclear Pore
  • Nuclear Proteins
  • Nucleocytoplasmic Transport Proteins
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • ran GTP-Binding Protein