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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.

Molecular cell | Sep 3, 2001

http://www.ncbi.nlm.nih.gov/pubmed/11583626

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 RIS Download

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