ArticleBiophysical journal2007
NMR studies in dodecylphosphocholine of a fragment containing the seventh transmembrane helix of a G-protein-coupled receptor from Saccharomyces cerevisiae.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 31 citations in OpenAlex.
- A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020Review
- Understanding GPCR Recognition and Folding from NMR Studies of Fragments.RSC advances · 2018Article
- Mycobacterium avium MAV_2941 mimics phosphoinositol-3-kinase to interfere with macrophage phagosome maturation.Microbes and infection · 2015Article
- Comparison of fragments comprising the first two helices of the human Y4 and the yeast Ste2p G-protein-coupled receptors.Biophysical journal · 2012Article
- An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization.Protein expression and purification · 2012Article
- Probing the caveolin-1 P132L mutant: critical insights into its oligomeric behavior and structure.Biochemistry · 2012Article
- Large multiple transmembrane domain fragments of a G protein-coupled receptor: biosynthesis, purification, and biophysical studies.Biopolymers · 2012Article
- Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.Biochimica et biophysica acta · 2011Article
- Structural and dynamic properties of juxta-membrane segments of caveolin-1 and caveolin-2 at the membrane interface.European biophysics journal : EBJ · 2010Article
- Identification of specific transmembrane residues and ligand-induced interface changes involved in homo-dimer formation of a yeast G protein-coupled receptor.Biochemistry · 2009Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Structure of a double transmembrane fragment of a G-protein-coupled receptor in micelles.Biophysical journal · 2009Article
- Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR.Journal of biomolecular NMR · 2008Article
- Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers.Biophysical journal · 2008Article
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5 authors at 4 institutions in 2 countries.
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Abstract
The structure and dynamics of a large segment of Ste2p, the G-protein-coupled alpha-factor receptor from yeast, were studied in dodecylphosphocholine (DPC) micelles using solution NMR spectroscopy. We investigated the 73-residue peptide EL3-TM7-CT40 consisting of the third extracellular loop 3 (EL3), the seventh transmembrane helix (TM7), and 40 residues from the cytosolic C-terminal domain (CT40). The structure reveals the presence of an alpha-helix in the segment encompassing residues 10-30, which is perturbed around the internal Pro-24 residue. Root mean-square deviation values of individually superimposed helical segments 10-20 and 25-30 were 0.91 +/- 0.33 A and 0.76 +/- 0.37 A, respectively. 15N-relaxation and residual dipolar coupling data support a rather stable fold for the TM7 part of EL3-TM7-CT40, whereas the EL3 and CT40 segments are more flexible. Spin-label data indicate that the TM7 helix integrates into DPC micelles but is flexible around the internal Pro-24 site, exposing residues 22-26 to solution and reveal a second site of interaction with the micelle within a region comprising residues 43-58, which forms part of a less well-defined nascent helix. These findings are discussed in light of previous studies in organic-aqueous solvent systems.
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