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- W2037260827 endingPage "269" @default.
- W2037260827 startingPage "257" @default.
- W2037260827 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." @default.
- W2037260827 created "2016-06-24" @default.
- W2037260827 creator A5008534508 @default.
- W2037260827 creator A5044184936 @default.
- W2037260827 creator A5049373174 @default.
- W2037260827 date "2008-10-21" @default.
- W2037260827 modified "2023-10-16" @default.
- W2037260827 title "Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR" @default.
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- W2037260827 doi "https://doi.org/10.1007/s10858-008-9281-z" @default.
- W2037260827 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18937032" @default.
- W2037260827 hasPublicationYear "2008" @default.
- W2037260827 type Work @default.