2HGM

NMR structure of the second qRRM domain of human hnRNP F

Summary for 2HGM

• Entry DOI: 10.2210/pdb2hgm/pdb
• Related: 2HGL 2HGN
• Descriptor: Heterogeneous nuclear ribonucleoprotein F (1 entity in total)
• Functional Keywords: rna recognition motif, g-tract, g-quadruplex, alternative splicing, rna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13781.41

Authors

Dominguez, C.,Allain, F.H.-T. (deposition date: 2006-06-27, release date: 2006-07-11, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR