Linked Life Data

11013258

Source:http://linkedlifedata.com/resource/pubmed/id/11013258

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-3-6
pubmed:abstractText
We mutated the vasoactive intestinal peptide (VIP) Asp(3) residue and two VPAC(1) receptor second transmembrane helix basic residues (Arg(188) and Lys(195)). VIP had a lower affinity for R188Q, R188L, K195Q, and K195I VPAC(1) receptors than for VPAC(1) receptors. [Asn(3)] VIP and [Gln(3)] VIP had lower affinities than VIP for VPAC(1) receptors but higher affinities for the mutant receptors; the two basic amino acids facilitated the introduction of the negatively charged aspartate inside the transmembrane domain. The resulting interaction was necessary for receptor activation. 1/[Asn(3)] VIP and [Gln(3)] VIP were partial agonists at VPAC(1) receptors; 2/VIP did not fully activate the K195Q, K195I, R188Q, and R188L VPAC(1) receptors; a VIP analogue ([Arg(16)] VIP) was more efficient than VIP at the four mutated receptors; and [Asn(3)] VIP and [Gln(3)] VIP were more efficient than VIP at the R188Q and R188L VPAC(1) receptors; 3/the [Asp(3)] negative charge did not contribute to the recognition of the VIP(1) antagonist, [AcHis(1),D-Phe(2),Lys(15),Arg(16),Leu(27)] VIP ()/growth hormone releasing factor (8-27). This is the first demonstration that, to activate the VPAC(1) receptor, the Asp(3) side chain of VIP must penetrate within the transmembrane domain, in close proximity to two highly conserved basic amino acids from transmembrane 2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1084-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11013258-Adenylate Cyclase, pubmed-meshheading:11013258-Amino Acid Substitution, pubmed-meshheading:11013258-Animals, pubmed-meshheading:11013258-CHO Cells, pubmed-meshheading:11013258-Cell Membrane, pubmed-meshheading:11013258-Cricetinae, pubmed-meshheading:11013258-Humans, pubmed-meshheading:11013258-Kinetics, pubmed-meshheading:11013258-Lysine, pubmed-meshheading:11013258-Mutagenesis, Site-Directed, pubmed-meshheading:11013258-Protein Structure, Secondary, pubmed-meshheading:11013258-Receptors, Vasoactive Intestinal Peptide, pubmed-meshheading:11013258-Receptors, Vasoactive Intestinal Polypeptide, Type I, pubmed-meshheading:11013258-Recombinant Proteins, pubmed-meshheading:11013258-Signal Transduction, pubmed-meshheading:11013258-Transfection, pubmed-meshheading:11013258-Vasoactive Intestinal Peptide
pubmed:year
2001
pubmed:articleTitle
Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction.
pubmed:affiliation
Laboratoire de Chimie Biologique et de la Nutrition, Faculté de Médecine, Université Libre de Bruxelles, 808 route de Lennik, Building G/E, CP 611, B-1070 Brussels, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't