Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helix.

doi:10.1038/sj.bjp.0704195

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Article

Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helix.

British journal of pharmacology - 1 Aug 2001

Vertongen P, Solano R M, Perret J, Langer I, Robberecht P, Waelbroeck M

Abstract excerpt

1. We investigated the role of two conserved basic residues in the second transmembrane helix arginine 172 (R172) and lysine 179 (K179) of the VPAC(2) receptor. 2. Vasoactive intestinal polypeptide (VIP) activated VPAC(2) receptors with an EC(50) value of 7 nM, as compared to 150, 190 and 4000 nM at R172L, R172Q and K179Q-VPAC(2) receptors, respectively. It was inactive at K179I mutated VPAC(2) receptors. These...

Topics

Acylation
Adenylyl Cyclases
Amino Acid Substitution
Animals
Arginine
CHO Cells
Cell Membrane
Cricetinae
Enzyme Activation
Humans
Lysine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Mutation

Protein Structure, Secondary

Receptors, Vasoactive Intestinal Peptide

Receptors, Vasoactive Intestinal Peptide, Type II

Recombinant Proteins

Structure-Activity Relationship

Source

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Identifiers

PMID: 11498510
DOI: 10.1038/sj.bjp.0704195
PMCID: PMC1621147

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