TY  - JOUR
AU  - Sonntag, Miriam
AU  - Jagtap, Pravin Kumar Ankush
AU  - Simon, Bernd
AU  - Appavou, Marie-Sousai
AU  - Geerlof, Arie
AU  - Stehle, Ralf
AU  - Gabel, Frank
AU  - Hennig, Janosch
AU  - Sattler, Michael
TI  - Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins
JO  - Angewandte Chemie / International edition
VL  - 56
IS  - 32
SN  - 1433-7851
CY  - Weinheim
PB  - Wiley-VCH
M1  - FZJ-2017-07361
SP  - 9322 - 9325
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28636238
UR  - <Go to ISI:>//WOS:000406385200010
DO  - DOI:10.1002/anie.201702904
UR  - https://juser.fz-juelich.de/record/838851
ER  -