Abstract
RGS10 is a member of the D/R12 subfamily of Regulators of G-protein Signalling (RGS) proteins and acts as a GTPase-activating protein (GAP) via modulation of Gαi and Gαz signalling but does not interact with the structurally distinct Gαs subunit (Hunt et al., 1996). Unlike other subfamilies of RGS proteins, RGS10 lacks the N-terminal ampipathic helix that localizes these proteins to the membrane. Instead, membrane localization is regulated by palmitoylation of a conserved cysteine within the GTPase-activating RGS domain (Tu et al., 1999). H, N and C resonance assignments of a construct containing the RGS domain from human RGS10 were obtained from 2D and 3D heteronuclear NMR spectra. The backbone assignment was completed with the exception of the first and last two residues and a highly overlapped stretch of five Glu residues (132-136 of our construct). Sidechain assignment was 89% complete including 92 % of observable aromatics. The assignments were deposited with accession code BMRB-7272.
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