1HO0
NEW B-CHAIN MUTANT OF BOVINE INSULIN
Summary for 1HO0
| Entry DOI | 10.2210/pdb1ho0/pdb |
| Descriptor | INSULIN (1 entity in total) |
| Functional Keywords | beta_turn (20-23), alpha_helix (9-19), hormone-growth factor complex, hormone/growth factor |
| Total number of polymer chains | 1 |
| Total formula weight | 3371.80 |
| Authors | Dupradeau, F.Y.,Richard, T.,Le Flem, G.,Oulyadi, H.,Prigent, Y.,Monti, J.P. (deposition date: 2000-12-08, release date: 2000-12-20, Last modification date: 2024-05-22) |
| Primary citation | Dupradeau, F.Y.,Richard, T.,Le Flem, G.,Oulyadi, H.,Prigent, Y.,Monti, J.P. A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure J.Pept.Res., 60:56-64, 2002 Cited by PubMed Abstract: 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. PubMed: 12081626DOI: 10.1034/j.1399-3011.2002.02990.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
