Segmental, domain-selective perdeuteration and small angle neutron scattering for structural analysis of multi-domain proteins.

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 re-arrangements 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 modelling 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.
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Article dans une revue
Angewandte Chemie (English Edition), John Wiley & Sons, 2017, 〈10.1002/anie.201702904〉
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http://hal.univ-grenoble-alpes.fr/hal-01549692
Contributeur : Frank Thomas <>
Soumis le : jeudi 29 juin 2017 - 09:20:36
Dernière modification le : jeudi 11 janvier 2018 - 06:15:24

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Miriam Sonntag, Pravin Jagtap, Bernd Simon, Marie-Sousai Appavou, Arie Geerlof, et al.. Segmental, domain-selective perdeuteration and small angle neutron scattering for structural analysis of multi-domain proteins.. Angewandte Chemie (English Edition), John Wiley & Sons, 2017, 〈10.1002/anie.201702904〉. 〈hal-01549692〉

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