This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1t0c
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1t0c.gif|left|200px]] | [[Image:1t0c.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1t0c", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1t0c| PDB=1t0c | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''Solution Structure of Human Proinsulin C-Peptide''' | '''Solution Structure of Human Proinsulin C-Peptide''' | ||
| Line 32: | Line 29: | ||
[[Category: Munte, C E.]] | [[Category: Munte, C E.]] | ||
[[Category: Vilela, L.]] | [[Category: Vilela, L.]] | ||
| - | [[Category: | + | [[Category: Bend]] |
| - | [[Category: | + | [[Category: Type i beta-turn]] |
| - | [[Category: | + | [[Category: Type iii' beta-turn]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:20:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:20, 3 May 2008
Solution Structure of Human Proinsulin C-Peptide
Contents |
Overview
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.
Disease
Known disease associated with this structure: Diabetes mellitus, rare form OMIM:[176730], Hyperproinsulinemia, familial OMIM:[176730], MODY, one form OMIM:[176730]
About this Structure
1T0C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human proinsulin C-peptide., Munte CE, Vilela L, Kalbitzer HR, Garratt RC, FEBS J. 2005 Aug;272(16):4284-93. PMID:16098208 Page seeded by OCA on Sat May 3 09:20:51 2008
