Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-12-15
pubmed:abstractText
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- y6) using segments and analogues of NPY. The Y1-, Y2- and the Y5-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 y6-receptor is truncated in human. In this review, we summarize the data of neuropeptide Y with respect to ligand binding, selectivity, receptor structures and ligand-receptor complexes by using ligand analogues, site directed mutagenesis and photoaffinity labeling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0929-8673
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1055-66
pubmed:dateRevised
2007-2-12
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Molecular characterization of the ligand-receptor interaction of neuropeptide Y.
pubmed:affiliation
Swiss Federal Institute of Technology Zürich, Department of Pharmacy, Winterthurer Str. 190, Zürich, CH 8057, Zürich.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't