1OAI

Complex between Tap UBA domain and FxFG nucleoporin peptide

1OAI の概要

• エントリーDOI: 10.2210/pdb1oai/pdb
• 分子名称: NUCLEAR RNA EXPORT FACTOR, FXFG NUCLEOPORIN PEPTIDE (3 entities in total)
• 機能のキーワード: nuclear transport, nuclear transport factor, nucleoporin
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7729.56

構造登録者

Grant, R.P.,Neuhaus, D.,Stewart, M. (登録日: 2003-01-14, 公開日: 2003-02-20, 最終更新日: 2024-05-08)

主引用文献

Grant, R.P.,Neuhaus, D.,Stewart, M.
Structural Basis for the Interaction between the Tap/Nxf1 Uba Domain and Fg Nucleoporins at 1 A Resolution
J.Mol.Biol., 326:849-, 2003

PubMed Abstract: The mRNA nuclear export function of Tap/NXF1 requires interactions with nuclear pore proteins (nucleoporins) that contain characteristic Phe-Gly repeats based on FG, GLFG or FxFG cores separated by hydrophilic linkers. FG-nucleoporins bind the two most C-terminal domains of Tap, which have NTF2 and UBA folds, respectively. We used a combination of NMR and X-ray crystallography to define the interaction interface between Tap UBA and FxFG nucleoporins and show that it involves primarily the two aromatic rings of the FxFG core that bind in a hydrophobic surface depression centred on Tap Cys588. NMR evidence indicates that the same depression mediates the binding of GLFG nucleoporins, which we confirmed by demonstrating competition between the two classes of repeat for binding to Tap UBA. Moreover, modification of Cys588 reduced the binding of Tap UBA to both GLFG and FxFG nucleoporins as well as to nuclear envelopes. These data underscore the central role of the conserved FG-nucleoporin repeat cores in binding to Tap UBA and indicate that functional differences between different classes of nucleoporins depend more on their spatial distribution in nuclear pores than on their binding to different sites on Tap UBA.

PubMed: 12581645
DOI: 10.1016/S0022-2836(02)01474-2

実験手法

X-RAY DIFFRACTION (1 Å)