2HGN
NMR structure of the third qRRM domain of human hnRNP F
Summary for 2HGN
| Entry DOI | 10.2210/pdb2hgn/pdb |
| Related | 2HGL 2HGM |
| 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) |
| Cellular location | Nucleus, nucleoplasm: P52597 |
| Total number of polymer chains | 1 |
| Total formula weight | 15061.64 |
| 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 Cited by 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: 16885237DOI: 10.1093/nar/gkl488 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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