2KFY

NMR structure of the first qRRM of hnRNP F in complex with AGGGAU G-tract RNA

Summary for 2KFY

• Entry DOI: 10.2210/pdb2kfy/pdb
• Related: 2HGL 2KG0 2KG1
• Descriptor: Heterogeneous nuclear ribonucleoprotein F, 5'-R(*AP*GP*GP*GP*AP*U)-3' (2 entities in total)
• Functional Keywords: protein-rna complex, g tract, splicing regulation, polyadenylation regulation, mrna processing, mrna splicing, nucleus, phosphoprotein, ribonucleoprotein, rna-binding, spliceosome, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens
• Cellular location: Nucleus, nucleoplasm: P52597
• Total number of polymer chains: 2
• Total formula weight: 16983.16

Authors

Allain, F.H.T.,Dominguez, C. (deposition date: 2009-03-02, release date: 2010-06-09, Last modification date: 2024-05-08)

Primary citation

Dominguez, C.,Fisette, J.F.,Chabot, B.,Allain, F.H.
Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.
Nat.Struct.Mol.Biol., 17:853-861, 2010

PubMed Abstract: The heterogeneous nuclear ribonucleoprotein (hnRNP) F is involved in the regulation of mRNA metabolism by specifically recognizing G-tract RNA sequences. We have determined the solution structures of the three quasi-RNA-recognition motifs (qRRMs) of hnRNP F in complex with G-tract RNA. These structures show that qRRMs bind RNA in a very unusual manner, with the G-tract 'encaged', making the qRRM a novel RNA binding domain. We defined a consensus signature sequence for qRRMs and identified other human qRRM-containing proteins that also specifically recognize G-tract RNAs. Our structures explain how qRRMs can sequester G-tracts, maintaining them in a single-stranded conformation. We also show that isolated qRRMs of hnRNP F are sufficient to regulate the alternative splicing of the Bcl-x pre-mRNA, suggesting that hnRNP F would act by remodeling RNA secondary and tertiary structures.

PubMed: 20526337
DOI: 10.1038/nsmb.1814

Experimental method

SOLUTION NMR