Receptor-bound conformation of alpha-peptide of transucin (G_t) is not stabilized by a 'pi-cation' interaction but by constrained lactam bridges between residues 341 and 350

摘要

Light-induced activation of rhodopsin (R) leads to its conformation change and the binding of transucin G_t.Synthetic G_talpha (340-350) peptide has been demonstrated to stabilize R as does G_t.The bound conformation of R-bound G_talpha (340-350) has been determined by TrNOE NMR measurements.