1JN5

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

Summary for 1JN5

• Entry DOI: 10.2210/pdb1jn5/pdb
• Related: 1JKG
• Descriptor: p15, TAP, FG-repeat (3 entities in total)
• Functional Keywords: ntf2-like domain, nucleoporin, fg-repeat, transport protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9UKK6; Nucleus, nucleoplasm: Q9UBU9
• Total number of polymer chains: 3
• Total formula weight: 44924.54

Authors

Fribourg, S.,Braun, I.C.,Izaurralde, E.,Conti, E. (deposition date: 2001-07-23, release date: 2001-10-17, Last modification date: 2023-10-25)

Primary citation

Fribourg, S.,Braun, I.C.,Izaurralde, E.,Conti, E.
Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.
Mol.Cell, 8:645-656, 2001

PubMed Abstract: 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: 11583626
DOI: 10.1016/S1097-2765(01)00348-3

Experimental method

X-RAY DIFFRACTION (2.8 Å)