Effect of the Phosphate Group with Different Negative Charges on the Conformation of Phosphorylated Ser/Thr-Pro Motif
| Autor: | Yan-Ting Guo, Yan-Mei Li, Yufen Zhao, Zhen-Tai Zhu |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
Hydrogen bond Chemistry Stereochemistry Bioengineering Peptide Phosphate Biochemistry Cis trans isomerization Analytical Chemistry enzymes and coenzymes (carbohydrates) Residue (chemistry) chemistry.chemical_compound Drug Discovery Molecular Medicine Phosphorylation Signal transduction Isomerization |
| Zdroj: | International Journal of Peptide Research and Therapeutics. 11:159-165 |
| ISSN: | 1573-3904 1573-3149 |
| DOI: | 10.1007/s10989-005-4710-2 |
| Popis: | Ser/Thr-Pro motif is a widespread phosphorylated site in proteins, and its reversible phosphorylation is an important regulatory progress in many cell cycles and signal transduction. Recent research reveals that phosphorylation affects the local conformation of the peptide and its binding with the substrate through peptidyl--prolyl cis/trans isomerization. In order to further explore the effect of the phosphate group with different charges, four model peptides containing non- and phosphorylated Ser/Thr-Pro motif were synthesized using the classical solid-phase method. 1H-NMR, TOCSY, and ROESY were employed to characterize the conformation of the model peptides in solution with different pH value and analyze the peptidyl--prolyl isomerization at a molecular level. The results demonstrate that phosphorylation increases the cis conformation in the peptide and the maximum cis/trans ratio is obtained when the phosphate group has two negative charges. Furthermore, the experiments prove that the phosphorylation introduces a hydrogen bond between the phosphate and the NH of Ser/Thr residue, and the charges of the phosphate affect certain conformations of the phosphorylated Ser/Thr-Pro motif. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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