1E8S

Alu domain of the mammalian SRP (potential Alu retroposition intermediate)

1E8S の概要

• エントリーDOI: 10.2210/pdb1e8s/pdb
• 関連するPDBエントリー: 1E8O
• 分子名称: SIGNAL RECOGNITION PARTICLE 9 KDA PROTEIN, SIGNAL RECOGNITION PARTICLE 14 KDA PROTEIN, 7SL RNA, 88-MER, ... (4 entities in total)
• 機能のキーワード: alu ribonucleoprotein particle, alu rnp assembly and dimerisation, translational control, alu retroposition
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm: P49458 P37108
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 50905.63

構造登録者

Weichenrieder, O.,Wild, K.,Strub, K.,Cusack, S. (登録日: 2000-09-29, 公開日: 2000-11-08, 最終更新日: 2024-05-08)

主引用文献

Weichenrieder, O.,Wild, K.,Strub, K.,Cusack, S.
Structure and Assembly of the Alu Domain of the Mammalian Signal Recognition Particle
Nature, 408:167-, 2000

PubMed Abstract: The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. It retards the ribosomal elongation of signal-peptide-containing proteins before their engagement with the translocation machinery in the endoplasmic reticulum. Here we report two crystal structures of the heterodimer SRP9/14 bound either to the 5' domain or to a construct containing both 5' and 3' domains. We present a model of the complete Alu domain that is consistent with extensive biochemical data. SRP9/14 binds strongly to the conserved core of the 5' domain, which forms a U-turn connecting two helical stacks. Reversible docking of the more weakly bound 3' domain might be functionally important in the mechanism of translational regulation. The Alu domain structure is probably conserved in other cytoplasmic ribonucleoprotein particles and retroposition intermediates containing SRP9/14-bound RNAs transcribed from Alu repeats or related elements in genomic DNA.

PubMed: 11089964
DOI: 10.1038/35041507

実験手法

X-RAY DIFFRACTION (4 Å)