1JKG

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

1JKG の概要

• エントリーDOI: 10.2210/pdb1jkg/pdb
• 関連するPDBエントリー: 1JN5
• 分子名称: p15, TAP (3 entities in total)
• 機能のキーワード: ntf2-like domain, transport protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q9UKK6; Nucleus, nucleoplasm: Q9UBU9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43847.43

構造登録者

Fribourg, S.,Braun, I.C.,Izaurralde, E.,Conti, E. (登録日: 2001-07-12, 公開日: 2001-10-17, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)