1ho0
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1ho0.jpg|left|200px]] | + | [[Image:1ho0.jpg|left|200px]] |
| - | + | ||
| - | '''NEW B-CHAIN MUTANT OF BOVINE INSULIN''' | + | {{Structure |
| + | |PDB= 1ho0 |SIZE=350|CAPTION= <scene name='initialview01'>1ho0</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NEW B-CHAIN MUTANT OF BOVINE INSULIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HO0 is a [ | + | 1HO0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO0 OCA]. |
==Reference== | ==Reference== | ||
| - | A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure., Dupradeau FY, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti JP, J Pept Res. 2002 Jul;60(1):56-64. PMID:[http:// | + | A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure., Dupradeau FY, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti JP, J Pept Res. 2002 Jul;60(1):56-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12081626 12081626] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dupradeau, F Y.]] | [[Category: Dupradeau, F Y.]] | ||
| Line 21: | Line 30: | ||
[[Category: beta_turn (20-23)]] | [[Category: beta_turn (20-23)]] | ||
| - | ''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 11:39:31 2008'' |
Revision as of 09:39, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NEW B-CHAIN MUTANT OF BOVINE INSULIN
Overview
The solution structure of a new B-chain mutant of bovine insulin, in which the cysteines B7 and B19 are replaced by two serines, has been determined by circular dichroism, 2D-NMR and molecular modeling. This structure is compared with that of the oxidized B-chain of bovine insulin [Hawkins et al. (1995) Int. J. Peptide Protein Res.46, 424-433]. Circular dichroism spectroscopy showed in particular that a higher percentage of helical secondary structure for the B-chain mutant is estimated in trifluoroethanol solution in comparison with the oxidized B-chain. 2D-NMR experiments confirmed, among multiple conformations, that the B-chain mutant presents defined secondary structures such as a alpha-helix between residues B9 and B19, and a beta-turn between amino acids B20 and B23 in aqueous trifluoroethanol. The 3D structures, which are consistent with NMR data and were obtained using a simulated annealing protocol, showed that the tertiary structure of the B-chain mutant is better resolved and is more in agreement with the insulin crystal structure than the oxidized B-chain structure described by Hawkins et al. An explanation could be the presence of two sulfonate groups in the oxidized insulin B-chain. Either by their charges and/or their size, such chemical groups could play a destructuring effect and thus could favor peptide flexibility and conformational averaging. Thus, this study provides new insights on the folding of isolated B-chains.
About this Structure
1HO0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure., Dupradeau FY, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti JP, J Pept Res. 2002 Jul;60(1):56-64. PMID:12081626
Page seeded by OCA on Thu Mar 20 11:39:31 2008
