1GO5

Structure of the C-terminal FG-binding domain of human Tap

1GO5 の概要

• エントリーDOI: 10.2210/pdb1go5/pdb
• 関連するPDBエントリー: 1FO1
• NMR情報: BMRB: 5364
• 分子名称: TIP ASSOCIATING PROTEIN (1 entity in total)
• 機能のキーワード: nuclear transport, mrna export, uba, nucleoporins
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7718.60

構造登録者

Grant, R.P.,Hurt, E.,Neuhaus, D.,Stewart, M. (登録日: 2001-10-18, 公開日: 2002-02-05, 最終更新日: 2024-05-15)

主引用文献

Grant, R.P.,Hurt, E.,Neuhaus, D.,Stewart, M.
Structure of the C-Terminal Fg-Nucleoporin Binding Domain of Tap/Nxf1
Nat.Struct.Biol., 9:247-, 2002

PubMed Abstract: The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four alpha-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.

PubMed: 11875519
DOI: 10.1038/NSB773

実験手法

SOLUTION NMR