1OWX

Solution structure of the C-terminal RRM of human La (La225-334)

1OWX の概要

• エントリーDOI: 10.2210/pdb1owx/pdb
• 分子名称: Lupus La protein (1 entity in total)
• 機能のキーワード: rrm, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (Probable): P05455
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13951.84

構造登録者

Jacks, A.,Babon, J.,Kelly, G.,Manolaridis, I.,Cary, P.D.,Curry, S.,Conte, M.R. (登録日: 2003-03-31, 公開日: 2003-07-29, 最終更新日: 2024-05-22)

主引用文献

Jacks, A.,Babon, J.,Kelly, G.,Manolaridis, I.,Cary, P.D.,Curry, S.,Conte, M.R.
Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element
Structure, 11:833-843, 2003

PubMed Abstract: The La protein is an important component of ribonucleoprotein complexes that acts mainly as an RNA chaperone to facilitate correct processing and maturation of RNA polymerase III transcripts, but can also stimulate translation initiation. We report here the structure of the C-terminal domain of human La, which comprises an atypical RNA recognition motif (La225-334) and a long unstructured C-terminal tail. The central beta sheet of La225-334 reveals novel features: the putative RNA binding surface is formed by a five-stranded beta sheet and, strikingly, is largely obscured by a long C-terminal alpha helix that encompasses a recently identified nuclear retention element. Contrary to previous observations, we find that the La protein does not contain a dimerization domain.

PubMed: 12842046
DOI: 10.1016/S0969-2126(03)00121-7

実験手法

SOLUTION NMR