Peptides corresponding to the N- and C-terminal parts of PEBP are well-structured in solution: new insights into their possible interaction with partners in vivo
| Autor: | Béatrice Vallée, Gael COADOU, Labbé, H., Sy, D., Vovelle, F., Schoentgen, F. |
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| Přispěvatelé: | LEGOUPIL, Laëtitia, Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Circular Dichroism [SDV]Life Sciences [q-bio] Molecular Sequence Data Sequence Homology Phosphatidylethanolamine Binding Protein Androgen-Binding Protein Peptide Fragments Solutions [SDV] Life Sciences [q-bio] Protein Interaction Mapping Animals Humans Cattle Amino Acid Sequence Phospholipid Transfer Proteins Carrier Proteins Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Journal of Peptide Research Journal of Peptide Research, Wiley-Blackwell, 2003, 61 (2), pp.47-57 HAL |
| ISSN: | 1397-002X 1399-3011 |
| Popis: | International audience; Recently, it has been shown that mammalian PEBPs are implicated in several signalling pathways controlling the cellular cycle. In particular, during brain development, the N-terminal part of mammalian PEBP is specifically cleaved and the resulting 11 amino acid peptide stimulates the growth and activity of acetylcholinergic neurons. The crystallographic structure of bovine and human PEBPs has revealed that their N- and C-terminal parts are accessible and exposed to the solvent suggesting that they may be involved in specific interactions with cellular partners. We have chemically synthetized the two peptides corresponding to these terminal parts and studied their structure in solution by circular dichroism and NMR spectroscopies: both of them are well-structured. The N-terminal peptide is composed of a series of turns, leading to a hook conformation. The C-terminal peptide displays a globally helical conformation similar to that observed in the whole protein; it is characterized by an amphipatic feature with a hydrophobic cluster located on one side. These structural features enlighten previous fluorescence and monolayer experiments and give new insights on the roles of both PEBP termini. |
| Databáze: | OpenAIRE |
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