1t0c: Difference between revisions
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[[Image:1t0c.gif|left|200px]] | [[Image:1t0c.gif|left|200px]] | ||
'''Solution Structure of Human Proinsulin C-Peptide''' | {{Structure | ||
|PDB= 1t0c |SIZE=350|CAPTION= <scene name='initialview01'>1t0c</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= INS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Solution Structure of Human Proinsulin C-Peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1T0C is a [ | 1T0C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0C OCA]. | ||
==Reference== | ==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:[http:// | Solution structure of human proinsulin C-peptide., Munte CE, Vilela L, Kalbitzer HR, Garratt RC, FEBS J. 2005 Aug;272(16):4284-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16098208 16098208] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: type iii' beta-turn]] | [[Category: type iii' beta-turn]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:12:02 2008'' | ||
Revision as of 12:12, 20 March 2008
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| Gene: | INS (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Solution Structure of Human Proinsulin C-Peptide
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 diseases 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 Thu Mar 20 14:12:02 2008
