Repository logo
 

NMR resonance assignments for the active and inactive conformations of the small G protein RalA.

Accepted version
Peer-reviewed

Type

Article

Change log

Authors

Shafiq, Arooj 
Campbell, Louise J 

Abstract

The Ral proteins (RalA and RalB) are small G proteins of the Ras family that have been implicated in exocytosis, endocytosis, transcriptional regulation and mitochondrial fission, as well as having a role in tumourigenesis. RalA and RalB are activated downstream of the master regulator, Ras, which causes the nucleotide exchange of GDP for GTP. Here we report the 1H, 15 N and 13C resonance assignments of RalA in its active form bound to the GTP analogue GMPPNP. We also report the backbone assignments of RalA in its inactive, GDP-bound form. The assignments give insight into the switch regions, which change conformation upon nucleotide exchange. These switch regions are invisible in the spectra of the active, GMPPNP bound form but the residues proximal to the switches can be monitored. RalA is also an important drug target due to its over activation in some cancers and these assignments will be extremely useful for NMR-based screening approaches.

Description

Keywords

G Protein, Gtpase, Ral, Ras, Signalling, Guanosine Diphosphate, Monomeric GTP-Binding Proteins, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, ral GTP-Binding Proteins

Journal Title

Biomol NMR Assign

Conference Name

Journal ISSN

1874-2718
1874-270X

Volume Title

14

Publisher

Springer Science and Business Media LLC

Rights

All rights reserved
Sponsorship
Medical Research Council (MR/J007803/1)
Medical Research Council (G0700057)