5O2V

NMR structure of TIA-1 RRM1 domain

5O2V の概要

• エントリーDOI: 10.2210/pdb5o2v/pdb
• NMR情報: BMRB: 34144
• 分子名称: Nucleolysin TIA-1 isoform p40 (1 entity in total)
• 機能のキーワード: rrm, tia-1, 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: 10275.84

構造登録者

Jagtap, P.K.A. (登録日: 2017-05-22, 公開日: 2017-06-28, 最終更新日: 2024-06-19)

主引用文献

Sonntag, M.,Jagtap, P.K.A.,Simon, B.,Appavou, M.S.,Geerlof, A.,Stehle, R.,Gabel, F.,Hennig, J.,Sattler, M.
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.
Angew. Chem. Int. Ed. Engl., 56:9322-9325, 2017

PubMed Abstract: Multi-domain proteins play critical roles in fine-tuning essential processes in cellular signaling and gene regulation. Typically, multiple globular domains that are connected by flexible linkers undergo dynamic rearrangements upon binding to protein, DNA or RNA ligands. RNA binding proteins (RBPs) represent an important class of multi-domain proteins, which regulate gene expression by recognizing linear or structured RNA sequence motifs. Here, we employ segmental perdeuteration of the three RNA recognition motif (RRM) domains in the RBP TIA-1 using Sortase A mediated protein ligation. We show that domain-selective perdeuteration combined with contrast-matched small-angle neutron scattering (SANS), SAXS and computational modeling provides valuable information to precisely define relative domain arrangements. The approach is generally applicable to study conformational arrangements of individual domains in multi-domain proteins and changes induced by ligand binding.

PubMed: 28636238
DOI: 10.1002/anie.201702904

実験手法

SOLUTION NMR