Structural Basis for the Recognition of a Nucleoporin FG Repeat by the NTF2-like Domain of the TAP/p15 mRNA Nuclear Export Factor
Copyright policy )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.
Models, Molecular, Nucleocytoplasmic Transport Proteins, Binding Sites, Recombinant Fusion Proteins, Molecular Sequence Data, Active Transport, Cell Nucleus, Nuclear Proteins, Cell Biology, Crystallography, X-Ray, Protein Structure, Tertiary, Mutagenesis, Site-Directed, Nuclear Pore, Animals, Humans, ATP-Binding Cassette Transporters, Amino Acid Sequence, RNA, Messenger, ATP Binding Cassette Transporter, Subfamily B, Member 2, Carrier Proteins, Molecular Biology, Dimerization, Protein Binding
Models, Molecular, Nucleocytoplasmic Transport Proteins, Binding Sites, Recombinant Fusion Proteins, Molecular Sequence Data, Active Transport, Cell Nucleus, Nuclear Proteins, Cell Biology, Crystallography, X-Ray, Protein Structure, Tertiary, Mutagenesis, Site-Directed, Nuclear Pore, Animals, Humans, ATP-Binding Cassette Transporters, Amino Acid Sequence, RNA, Messenger, ATP Binding Cassette Transporter, Subfamily B, Member 2, Carrier Proteins, Molecular Biology, Dimerization, Protein Binding
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