1OPI

SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE

1OPI の概要

• エントリーDOI: 10.2210/pdb1opi/pdb
• 関連するPDBエントリー: 1O0P
• 分子名称: SPLICING FACTOR U2AF 65 KDA SUBUNIT, SPLICING FACTOR SF1 (2 entities in total)
• 機能のキーワード: non-canonical rna recognition motif, 4-stranded anti-parallel beta-sheet, 2 alpha helices additionally extended by a third helix c, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P26368 Q15637
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13668.55

構造登録者

Selenko, P.,Gregorovic, G.,Sprangers, R.,Stier, G.,Rhani, Z.,Kramer, A.,Sattler, M. (登録日: 2003-03-05, 公開日: 2004-03-16, 最終更新日: 2024-05-22)

主引用文献

Selenko, P.,Gregorovic, G.,Sprangers, R.,Stier, G.,Rhani, Z.,Kramer, A.,Sattler, M.
Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
Mol.Cell, 11:965-976, 2003

PubMed Abstract: The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.

PubMed: 12718882
DOI: 10.1016/S1097-2765(03)00115-1

実験手法

SOLUTION NMR