2hgn
From Proteopedia
|
NMR structure of the third qRRM domain of human hnRNP F
Overview
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.
About this Structure
2HGN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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., Dominguez C, Allain FH, Nucleic Acids Res. 2006 Aug 2;34(13):3634-45. Print 2006. PMID:16885237
Page seeded by OCA on Mon Nov 12 22:32:13 2007
