Binding specificity of the ectodomain of the parathyroid hormone receptor
| Autor: | Eva Bosse-Doenecke, Rainer Rudolph, Mohanraj Gopalswamy, Jochen Balbach, Nils Drechsler, Günther Jahreis, Julia Fröbel |
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| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy Chemistry Parathyroid hormone receptor Molecular Sequence Data Organic Chemistry Biophysics Parathyroid hormone Isothermal titration calorimetry Peptide Peptide binding Calorimetry Biochemistry Recombinant Proteins Protein Structure Tertiary Ectodomain Humans Amino Acid Sequence Receptor hormones hormone substitutes and hormone antagonists Protein Binding Receptor Parathyroid Hormone Type 1 G protein-coupled receptor |
| Zdroj: | Biophysical Chemistry. 154:66-72 |
| ISSN: | 0301-4622 |
| DOI: | 10.1016/j.bpc.2011.01.002 |
| Popis: | The parathyroid hormone (PTH)1 receptor is a member of the class B G protein-coupled receptor (GPCR) family and regulates bone and mineral metabolism of vertebrates. A truncated highly active parathyroid hormone fragment PTH (1–34) exerts stimulatory effects on the receptor and is used for treatment of osteoporosis. To study the interacting amino acids of the natural peptide ligand PTH (1–84) with the ectodomain of its receptor we used peptide micro arrays on solid cellulose membranes. The amino acids Arg20 and Trp23 within the identified core binding stretch PTH (20–26) were found to be most important for affinity to the ectodomain of PTH1R. Isothermal titration calorimetry and NMR spectroscopy allowed peptide binding studies in solution and verified peptide positions required for high affinity. With this combination of biochemical and biophysical methods we extend former findings on this essential interaction and can now provide a strategy to screen for optimized therapeutic peptides. |
| Databáze: | OpenAIRE |
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