ArticleJournal of biomolecular NMR2008
Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR.
Article in Journal of biomolecular NMR, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 17 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
- Small expression tags enhance bacterial expression of the first three transmembrane segments of the apelin receptor.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2014Article
- Guided reconstitution of membrane protein fragments.Biopolymers · 2014Article
- 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
- Large multiple transmembrane domain fragments of a G protein-coupled receptor: biosynthesis, purification, and biophysical studies.Biopolymers · 2012Article
- 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
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The human Y4 receptor, a class A G-protein coupled receptor (GPCR) primarily targeted by the pancreatic polypeptide (PP), is involved in a large number of physiologically important functions. This paper investigates a Y4 receptor fragment (N-TM1-TM2) comprising the N-terminal domain, the first two transmembrane (TM) helices and the first extracellular loop followed by a (His)(6) tag, and addresses synthetic problems encountered when recombinantly producing such fragments from GPCRs in Escherichia coli. Rigorous purification and usage of the optimized detergent mixture 28 mM dodecylphosphocholine (DPC)/118 mM% 1-palmitoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] (LPPG) resulted in high quality TROSY spectra indicating protein conformational homogeneity. Almost complete assignment of the backbone, including all TM residue resonances was obtained. Data on internal backbone dynamics revealed a high secondary structure content for N-TM1-TM2. Secondary chemical shifts and sequential amide proton nuclear Overhauser effects defined the TM helices. Interestingly, the properties of the N-terminal domain of this large fragment are highly similar to those determined on the isolated N-terminal domain in the presence of DPC micelles.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.