1FT8

CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE MRNA EXPORT FACTOR TAP

1FT8 の概要

• エントリーDOI: 10.2210/pdb1ft8/pdb
• 関連するPDBエントリー: 1FO1
• 分子名称: TIP ASSOCIATING PROTEIN (1 entity in total)
• 機能のキーワード: ribonucleoprotein (rnp, rrm, rbd) and leucine-rich-repeat (lrr) domains, rna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 154011.08

構造登録者

Liker, E.,Fernandez, E.,Izaurralde, E.,Conti, E. (登録日: 2000-09-12, 公開日: 2000-12-11, 最終更新日: 2024-02-07)

主引用文献

Liker, E.,Fernandez, E.,Izaurralde, E.,Conti, E.
The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain.
EMBO J., 19:5587-5598, 2000

PubMed Abstract: Human TAP is implicated in mRNA nuclear export and is used by simian type D retroviruses to export their unspliced genomic RNA to the cytoplasm of the host cell. We have determined the crystal structure of the minimal TAP fragment that binds the constitutive transport element (CTE) of retroviral RNAs. Unexpectedly, we find the fragment consists of a ribonucleoprotein (RNP) domain, which is not identifiable by its sequence, and a leucine-rich repeat (LRR) domain. The non-canonical RNP domain functions as the general RNA-binding portion of the fragment. The LRR domain is required in cis to the RNP domain for CTE RNA binding. The structural and biochemical properties of the domains point to a remarkable similarity with the U2B"(RNP)-U2A'(LRR) spliceosomal heterodimer. Our in vitro and in vivo functional studies using structure-based mutants suggest that a phylogenetically conserved surface of the LRR domain of TAP may have different roles in the export of viral and cellular RNAs.

PubMed: 11060011
DOI: 10.1093/emboj/19.21.5587

実験手法

X-RAY DIFFRACTION (3.15 Å)