Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-3-12
pubmed:abstractText
The contribution of the extracellular loops of the secretin receptor to the recognition of secretin was investigated by transfection in CHO cells of chimeric receptors, in which the three loops of the secretin recombinant receptor were replaced by the corresponding sequences of the glucagon receptor. The role of the third loop could not be evaluated as the transfected cells did not respond to secretin. Replacement of extracellular loop 2 reduced markedly the capability of secretin to occupy the receptor but did not alter the capacity of the receptor to discriminate between peptide analogues modified in position 3. Replacement of the first extracellular loop not only reduced the potency of secretin but also decreased the capacity of the receptor to discriminate between ligands having in position 3 an aspartate (as in secretin), an asparagine, or a glutamic acid. This change in receptor properties was reproduced by a single mutation of lysine 173 of the receptor into isoleucine. Thus, the basic amino acid in position 173 is likely to interact with aspartate 3 of secretin. As an aspartate is also present in position 3 of VIP and PACAP, two peptides related to secretin, and a lysine residue is conserved in the first extracellular loop of the VIP and PACAP receptors, this interaction may be a key element of peptide recognition by this receptor family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
842-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8579602-Adenylate Cyclase, pubmed-meshheading:8579602-Amino Acid Sequence, pubmed-meshheading:8579602-Animals, pubmed-meshheading:8579602-Aspartic Acid, pubmed-meshheading:8579602-Extracellular Space, pubmed-meshheading:8579602-Ligands, pubmed-meshheading:8579602-Lysine, pubmed-meshheading:8579602-Molecular Sequence Data, pubmed-meshheading:8579602-Rats, pubmed-meshheading:8579602-Receptors, G-Protein-Coupled, pubmed-meshheading:8579602-Receptors, Gastrointestinal Hormone, pubmed-meshheading:8579602-Receptors, Glucagon, pubmed-meshheading:8579602-Recombinant Fusion Proteins, pubmed-meshheading:8579602-Secretin, pubmed-meshheading:8579602-Sequence Alignment, pubmed-meshheading:8579602-Sequence Homology, Amino Acid, pubmed-meshheading:8579602-Structure-Activity Relationship
pubmed:year
1996
pubmed:articleTitle
Lysine 173 residue within the first exoloop of rat secretin receptor is involved in carboxylate moiety recognition of Asp 3 in secretin.
pubmed:affiliation
Department of Biochemistry and Nutrition, School of Medicine, Université Libre de Bruxelles, Belgium.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't