1JMT

X-ray Structure of a Core U2AF65/U2AF35 Heterodimer

1JMT の概要

• エントリーDOI: 10.2210/pdb1jmt/pdb
• 分子名称: SPLICING FACTOR U2AF 35 KDA SUBUNIT, SPLICING FACTOR U2AF 65 KDA SUBUNIT, HEXANE-1,6-DIOL, ... (4 entities in total)
• 機能のキーワード: rrm, rna splicing, proline, ppii helix, peptide recognition, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15657.47

構造登録者

Kielkopf, C.L.,Rodionova, N.A.,Green, M.R.,Burley, S.K. (登録日: 2001-07-19, 公開日: 2001-09-19, 最終更新日: 2024-02-07)

主引用文献

Kielkopf, C.L.,Rodionova, N.A.,Green, M.R.,Burley, S.K.
A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer.
Cell(Cambridge,Mass.), 106:595-605, 2001

PubMed Abstract: U2 auxiliary factor (U2AF) is an essential splicing factor that recognizes the 3' splice site and recruits the U2 snRNP to the branch point. The X-ray structure of the human core U2AF heterodimer, consisting of the U2AF35 central domain and a proline-rich region of U2AF65, has been determined at 2.2 A resolution. The structure reveals a novel protein-protein recognition strategy, in which an atypical RNA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tongue-in-groove" tryptophan residues. Complementary biochemical experiments demonstrate that the core U2AF heterodimer binds RNA, and that the interacting tryptophan side chains are essential for U2AF dimerization. Atypical RRMs in other splicing factors may serve as protein-protein interaction motifs elsewhere during spliceosome assembly.

PubMed: 11551507
DOI: 10.1016/S0092-8674(01)00480-9

実験手法

X-RAY DIFFRACTION (2.2 Å)