6DG1

NMR structure of the second qRRM2 domain of human hnRNP H

6DG1 の概要

• エントリーDOI: 10.2210/pdb6dg1/pdb
• NMR情報: BMRB: 30469
• 分子名称: qRRM2 domain of Heterogeneous nuclear ribonucleoprotein H2 (1 entity in total)
• 機能のキーワード: hnrnp h, heterogeneous nuclear ribonucleoprotein h, hqrrm2, qrrm2, rna binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11791.32

構造登録者

Srinivasa, R.P. (登録日: 2018-05-16, 公開日: 2018-09-05, 最終更新日: 2024-05-15)

主引用文献

Penumutchu, S.,Chiu, L.Y.,Meagher, J.L.,Hansen, A.L.,Stuckey, J.A.,Tolbert, B.S.
Differential Conformational Dynamics Encoded by the Inter-qRRM linker of hnRNP H.
J. Am. Chem. Soc., 2018

PubMed Abstract: Members of the heterogeneous nuclear ribonucleoprotein (hnRNP) F/H family are multipurpose 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 indicates 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.

PubMed: 30122033
DOI: 10.1021/jacs.8b05366

実験手法

SOLUTION NMR