TY - JOUR
T1 - Mutational analysis of the R33-encoded G protein-coupled receptor of rat cytomegalovirus: identification of amino acid residues critical for cellular localization and ligand-independent signalling
AU - Gruijthuijsen, Y.K.
AU - Beuken, E.V.
AU - Smit, M.J.
AU - Leurs, R.
AU - Bruggeman, C.A.
AU - Vink, C.
PY - 2004
Y1 - 2004
N2 - The rat cytomegalovirus (RCMV) R33 gene encodes a G protein-coupled receptor (GPCR), pR33, which possesses agonist-independent, constitutive signalling activity. To characterize this activity further, we generated a series of point and deletion mutants of pR33. Both expression of and signalling by the mutants was evaluated. Several point mutants were generated that contained modifications in the NRY motif. This motif, at aa 130-132 of pR33, is the counterpart of the common DRY motif of GPCRs, which is known to be involved in G protein coupling. We found that mutation of the asparagine residue within the NRY motif of pR33 (N
AB - The rat cytomegalovirus (RCMV) R33 gene encodes a G protein-coupled receptor (GPCR), pR33, which possesses agonist-independent, constitutive signalling activity. To characterize this activity further, we generated a series of point and deletion mutants of pR33. Both expression of and signalling by the mutants was evaluated. Several point mutants were generated that contained modifications in the NRY motif. This motif, at aa 130-132 of pR33, is the counterpart of the common DRY motif of GPCRs, which is known to be involved in G protein coupling. We found that mutation of the asparagine residue within the NRY motif of pR33 (N
U2 - 10.1099/vir.0.19709-0
DO - 10.1099/vir.0.19709-0
M3 - Article
SN - 0022-1317
VL - 85
SP - 897
EP - 909
JO - Journal of General Virology
JF - Journal of General Virology
IS - Pt 4
ER -