Fig. 5: Structure of the arrestin2-V2Rpp-6-7 complex.
From: Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2
a Structural alterations around sites V6 and V7 in the arrestin2-V2Rpp-6-7 complex structure (blue). Compared to the arrestin2-V2Rpp-FP complex, loss of pS363 and pS364 in V2Rpp-6-7 caused rotations of the side chains of direct phospho-contacting residues, such as K10, Y21, and K107, as well as structural reorganization at the N-terminal β sheet and α1 helix. The orange balls indicate that the phosphorylated peptide remains bound to arrestin, the green balls indicate loss of the original interaction of the phospho-residue. b Overall structural comparisons of arrestin2-V2Rpp-6-7 (slate) with the arrestin2-V2Rpp-FP complex (PDB: 4JQI, light cyan) and inactive arrestin2 (PDB:1G4M, gray). K49TMSiPhe was marked as orange ball. c The side chains of L48 and E50 at the NLS site in the arrestin2-V2Rpp-6-7 complex flipped towards the solvent compared with the same residues in the arrestin2-V2Rpp-FP complex. d Structural comparisons of the back loop in V2Rpp-6-7 bound arrestin2. e Structural rearrangement at the P1 region in the arrestin2-V2Rpp-6-7 complex. f 1D 1H NMR spectra of arrestin2-K49TMSiPhe incubated with different phosphopeptides.
