Munte, Claudia Elisabeth and Vilela, Luciano and Kalbitzer, Hans Robert and Garratt, Richard Charles (2005) Solution structure of human proinsulin C-peptide. FEBS JOURNAL, 272 (16). pp. 4284-4293. ISSN 1742-464X, 1742-4658
Full text not available from this repository. (Request a copy)Abstract
The C-peptide of proinsulin is important for the biosynthesis of insulin, but has been considered for a long time to be biologically inert. Recent studies in diabetic patients have stimulated a new debate about its possible regulatory role, suggesting that it is a hormonally active peptide. We describe structural studies of the C-peptide using 2D NMR spectroscopy. In aqueous solution, the NOE patterns and chemical shifts indicate that the ensemble is a nonrandom structure and contains substructures with defined local conformations. These are more clearly visible in 50% H2O/50% 2,2,2-trifluoroethanol. The N-terminal region (residues 2-5) forms a type I beta-turn, whereas the C-terminal region (residues 27-31) presents the most well-defined structure of the whole molecule including a type III' beta-turn. The C-terminal pentapeptide (EGSLQ) has been suggested to be responsible for chiral interactions with an as yet uncharacterized, probably a G-protein-coupled, receptor. The three central regions of the molecule (residues 9-12, 15-18 and 22-25) show tendencies to form beta-bends. We propose that the structure described here for the C-terminal pentapeptide is consistent with the previously postulated CA knuckle, believed to represent the active site of the C-peptide of human proinsulin.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HUMAN CELL-MEMBRANES; K+-ATPASE ACTIVITY; INSULIN; NMR; SPECTROSCOPY; MICROCIRCULATION; DYSFUNCTION; PRECURSOR; PROTEINS; SPECTRA; CA knuckle; NMR; proinsulin C-peptide; protein secondary structure |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 03 May 2021 06:11 |
| Last Modified: | 03 May 2021 06:11 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35797 |
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