6dg1 | pdb_00006dg1

NMR structure of the second qRRM2 domain of human hnRNP H

spinqualitylabelsall models 6dg1, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dg1 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: HNRNPH2, FTP3, HNRPH2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HNRH2_HUMAN] This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG). Publication Abstract from PubMed Members of the heterogeneous nuclear ribonucleoprotein (hnRNP) F/H family are multi purpose RNA binding proteins that participate in most stages of RNA metabolism. Despite having similar RNA sequence preferences, hnRNP F/H proteins function in overlapping and in some cases distinct cellular processes. The domain organization of hnRNP F/H proteins is modular consisting of N-terminal tandem quasi-RNA Recognition Motifs (F/HqRRM1,2) and a third C-terminal qRRM3 embedded between glycine-rich repeats. The tandem qRRMs are connected through a 10-residue linker with several amino acids strictly conserved between hnRNP H and F. A significant difference occurs at position 105 of the linker where hnRNP H contains a proline and hnRNP F an alanine. To investigate the influence of P105 on the conformational properties of hnRNP H, we probed the structural dynamics of its HqRRM1,2 domain with x-ray crystallography, NMR spectroscopy, and small angle x-ray scattering. The collective results best describe that HqRRM1,2 exists in a conformational equilibrium between compact and extended structures. The compact structure displays an electropositive surface formed at the qRRM1-qRRM2 interface. Comparison of NMR relaxation parameters, including Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion, between HqRRM1,2 and FqRRM1,2 indicate that FqRRM1,2 primarily adopts a more extended and flexible conformation. Introducing the P105A mutation into HqRRM1,2 alters its conformational dynamics to favor an extended structure. Thus, our work demonstrates that the linker compositions confer different structural properties between hnRNP F/H family members that might contribute to their functional diversity. Differential Conformational Dynamics Encoded by the Inter-qRRM linker of hnRNP H.,Penumutchu S, Chiu LY, Meagher JL, Hansen AL, Stuckey JA, Tolbert BS J Am Chem Soc. 2018 Aug 18. doi: 10.1021/jacs.8b05366. PMID:30122033 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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