ArticleBiochemistry2010
Binding of fluorinated phenylalanine alpha-factor analogues to Ste2p: evidence for a cation-pi binding interaction between a peptide ligand and its cognate G protein-coupled receptor.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- a-Factor: a chemical biology tool for the study of protein prenylation.Current topics in peptide & protein research · 2017Article
- Identification of destabilizing and stabilizing mutations of Ste2p, a G protein-coupled receptor in Saccharomyces cerevisiae.Biochemistry · 2015Article
- Guided reconstitution of membrane protein fragments.Biopolymers · 2014Article
- Fluorescent approaches for understanding interactions of ligands with G protein coupled receptors.Biochimica et biophysica acta · 2014Review
- Correlation between biological activity and binding energy in systems of integrin with cyclic RGD-containing binders: a QM/MM molecular dynamics study.Journal of molecular modeling · 2012Article
- Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.Biochimica et biophysica acta · 2011Article
- Biophysical characterization of G-protein coupled receptor-peptide ligand binding.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2011Review
- Identification of residue-to-residue contact between a peptide ligand and its G protein-coupled receptor using periodate-mediated dihydroxyphenylalanine cross-linking and mass spectrometry.The Journal of biological chemistry · 2010Article
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Authors and funding
5 authors at 4 institutions in 1 country.
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Abstract
Ste2p, a G protein-coupled receptor (GPCR), binds alpha-factor, WHWLQLKPGQPMY, a tridecapeptide pheromone secreted by yeast cells. Upon alpha-factor binding, Ste2p undergoes conformational changes activating a signal transduction system through its associated heterotrimeric G protein leading to the arrest of cell growth in the G1 phase to prepare cells for mating. Previous studies have indicated that Tyr at position 13 of alpha-factor interacts with Arg58 on transmembrane one (TM1) of Ste2p. This observation prompted this investigation to determine whether a cation-pi type of interaction occurred between these residues. Tyrosine at position 13 of alpha-factor was systematically substituted with analogous amino acids with varying cation-pi binding energies using solid-phase peptide synthesis, and these analogues were modified by derivatization of their Lys(7) residue with the fluorescent group 7-nitrobenz-2-oxa-1,3-diazole (NBD) to serve as a useful probe for binding determination. Saturation binding of these peptides to Ste2p was assayed using whole yeast cells and a flow cytometer. In parallel the biological activities of the peptides were determined using a growth arrest assay. The data provide evidence for the presence of a cation-pi interaction between Arg58 of Ste2p and Tyr(13) of alpha-factor.
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