N. Ingenhoven et Ag. Beck-sickinger, Molecular characterization of the ligand-receptor interaction of neuropeptide Y, CURR MED CH, 6(11), 1999, pp. 1055-1066
Neuropeptide Y (NPY) consists of 36 amino acids and is one of the most abun
dant peptides in the peripheral and central nervous system. Several subtype
s of NPY receptors have been described (Y-1 - y(6)) using segments and anal
ogues of NPY. The Y-1-, Y-2- and the Y-5-receptor, which have been cloned,
belong to the G-protein coupled hormone receptor family and will be special
ly addressed, because they are the endogenous binding sites of neuropeptide
Y in human. In contrast, Y-4-receptors recognize endogenous PP, Y-3-recept
ors are discussed controversially and the ys-receptor is truncated in human
. In this review, we summarize the data of neuropeptide Y with respect to l
igand binding, selectivity, receptor structures and ligand-receptor complex
es by using ligand analogues, site directed mutagenesis and photoaffinity l
abeling.