[HTML][HTML] Molecular characterization of the ligand-receptor interaction of neuropeptide Y

N Ingenhoven, AG Beck-Sickinger - Current medicinal chemistry, 1999 - books.google.com
N Ingenhoven, AG Beck-Sickinger
Current medicinal chemistry, 1999books.google.com
Neuropeptide Y (NPY) consists of 36 amino acids and is one of the most abundant peptides
in the peripheral and central nervous system. Several subtypes of NPY receptors have been
described (Y1-ye) using segments and analogues of NPY. The Y1-, Y2-and the Ys-receptor,
which have been cloned, belong to the G-protein coupled hormone receptor family and will
be specially addressed, because they are the endogenous binding sites of neuropeptide Y
in human. In contrast, Y4-receptors recognize endogenous PP, Y3-receptors are discussed …
Abstract
Neuropeptide Y (NPY) consists of 36 amino acids and is one of the most abundant peptides in the peripheral and central nervous system. Several subtypes of NPY receptors have been described (Y1-ye) using segments and analogues of NPY. The Y1-, Y2-and the Ys-receptor, which have been cloned, belong to the G-protein coupled hormone receptor family and will be specially addressed, because they are the endogenous binding sites of neuropeptide Y in human. In contrast, Y4-receptors recognize endogenous PP, Y3-receptors are discussed controversially and the ye-receptor is truncated in human. In this review, we summarize the data of neuropeptide Y with respect to ligand binding, selectivity, receptor structures and ligandreceptor complexes by using ligand analogues, site directed mutagenesis and photoaffinity labeling.
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