2HGL

NMR structure of the first qRRM domain of human hnRNP F

2HGL の概要

• エントリーDOI: 10.2210/pdb2hgl/pdb
• 関連するPDBエントリー: 2HGM 2HGN
• 分子名称: Heterogeneous nuclear ribonucleoprotein F (1 entity in total)
• 機能のキーワード: rna recognition motif, g-tract, g-quadruplex, alternative, splicing, rna binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15027.92

構造登録者

Dominguez, C.,Allain, F.H.-T. (登録日: 2006-06-27, 公開日: 2006-07-11, 最終更新日: 2024-05-01)

主引用文献

Dominguez, C.,Allain, F.H.
NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition.
Nucleic Acids Res., 34:3634-3645, 2006

PubMed Abstract: The heterogeneous nuclear ribonucleoprotein (hnRNP) F belongs to the hnRNP H family involved in the regulation of alternative splicing and polyadenylation and specifically recognizes poly(G) sequences (G-tracts). In particular, hnRNP F binds a G-tract of the Bcl-x RNA and regulates its alternative splicing, leading to two isoforms, Bcl-x(S) and Bcl-x(L), with antagonist functions. In order to gain insight into G-tract recognition by hnRNP H members, we initiated an NMR study of human hnRNP F. We present the solution structure of the three quasi RNA recognition motifs (qRRMs) of hnRNP F and identify the residues that are important for the interaction with the Bcl-x RNA by NMR chemical shift perturbation and mutagenesis experiments. The three qRRMs exhibit the canonical betaalphabetabetaalphabeta RRM fold but additional secondary structure elements are present in the two N-terminal qRRMs of hnRNP F. We show that qRRM1 and qRRM2 but not qRRM3 are responsible for G-tract recognition and that the residues of qRRM1 and qRRM2 involved in G-tract interaction are not on the beta-sheet surface as observed for the classical RRM but are part of a short beta-hairpin and two adjacent loops. These regions define a novel interaction surface for RNA recognition by RRMs.

PubMed: 16885237
DOI: 10.1093/nar/gkl488

実験手法

SOLUTION NMR