1JY6
B4DIMERA: A DE NOVO DESIGNED FOUR-STRANDED BETA-SHEET ASSEMBLED USING A DISULFIDE BOND
Summary for 1JY6
| Entry DOI | 10.2210/pdb1jy6/pdb |
| Related | 1JY4 |
| Descriptor | B4DIMER (1 entity in total) |
| Functional Keywords | four-stranded beta-sheet, disulfide bond, de novo protein design, de novo protein |
| Total number of polymer chains | 2 |
| Total formula weight | 7875.27 |
| Authors | Venkatraman, J.,Nagana Gowda, G.A.,Balaram, P. (deposition date: 2001-09-11, release date: 2002-06-12, Last modification date: 2024-10-30) |
| Primary citation | Venkatraman, J.,Nagana Gowda, G.A.,Balaram, P. Design and construction of an open multistranded beta-sheet polypeptide stabilized by a disulfide bridge. J.Am.Chem.Soc., 124:4987-4994, 2002 Cited by PubMed Abstract: The design and characterization of an open eight-stranded beta-sheet in a synthetic, 2-fold symmetric 70-residue peptide is described. The design strategy involves the generation of a 35-residue four-stranded beta-sheet peptide in which successive hairpins are nucleated by appropriately positioned (D)Pro-Xxx sequences. Oxidative dimerization using a single Cys residue positioned at the center of the C-terminal strand results in a disulfide-bridged eight-stranded structure. Nuclear Overhauser effects firmly establish an eight-stranded beta-sheet in methanol. In water, the outer strands are frayed, but a well-defined four-stranded beta-sheet stabilized by a disulfide bridge and a hydrophobic cluster is determined from NMR data. Comparison of the precursor peptide with the disulfide-bridged dimer reveals considerable enhancement of beta-sheet content in the latter, suggesting that the disulfide cross-link is an effective strategy for the stabilization of beta-sheets. PubMed: 11982362DOI: 10.1021/ja0174276 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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