4WYK

Structure of the LRR and NTF2-like domains of NXF1 complexed with NXT1

4WYK の概要

• エントリーDOI: 10.2210/pdb4wyk/pdb
• 分子名称: Nuclear RNA export factor 1, NTF2-related export protein 1 (2 entities in total)
• 機能のキーワード: nuclear export, transport protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus, nucleoplasm : Q9UBU9; Nucleus: Q9UKK6
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 135627.68

構造登録者

Aibara, S.,Valkov, E.,Stewart, M. (登録日: 2014-11-17, 公開日: 2015-02-04, 最終更新日: 2024-05-08)

主引用文献

Aibara, S.,Katahira, J.,Valkov, E.,Stewart, M.
The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA.
Nucleic Acids Res., 43:1883-1893, 2015

PubMed Abstract: The NXF1:NXT1 complex (also known as TAP:p15) is a general mRNA nuclear export factor that is conserved from yeast to humans. NXF1 is a modular protein constructed from four domains (RRM, LRR, NTF2-like and UBA domains). It is currently unclear how NXF1:NXT1 binds transcripts and whether there is higher organization of the NXF1 domains. We report here the 3.4 Å resolution crystal structure of the first three domains of human NXF1 together with NXT1 that has two copies of the complex in the asymmetric unit arranged to form an intimate domain-swapped dimer. In this dimer, the linkers between the NXF1 LRR and NTF2-like domains interact with NXT1, generating a 2-fold symmetric platform in which the RNA-binding RRM, LRR and NTF2-like domains are arranged on one face. In addition to bulk transcripts, NXF1:NXT1 also facilitates the export of unspliced retroviral genomic RNA from simple type-D retroviruses such as SRV-1 that contain a constitutive transport element (CTE), a cis-acting 2-fold symmetric RNA stem-loop motif. Complementary structural, biochemical and cellular techniques indicated that the formation of a symmetric RNA binding platform generated by dimerization of NXF1:NXT1 facilitates the recognition of CTE-RNA and promotes its nuclear export.

PubMed: 25628361
DOI: 10.1093/nar/gkv032

実験手法

X-RAY DIFFRACTION (3.4 Å)