2MOA
Solution NMR structure of peptide ImI1 (peak 2)
Summary for 2MOA
| Entry DOI | 10.2210/pdb2moa/pdb |
| Related | 1CNL 1E74 1G2G 1IM1 1IMI 2BC7 2C9T 4OS1 4OS2 4OS4 4OS5 4OS6 4OS7 |
| NMR Information | BMRB: 19932 |
| Related PRD ID | PRD_001232 |
| Descriptor | Alpha-conotoxin ImI (1 entity in total) |
| Functional Keywords | dithiol amino acid, conotoxin, bicyclic peptide, macrocycle, phage display, toxin |
| Biological source | Conus imperialis (Imperial cone) |
| Cellular location | Secreted: P50983 |
| Total number of polymer chains | 1 |
| Total formula weight | 1384.65 |
| Authors | Heinis, C.,Chen, S. (deposition date: 2014-04-24, release date: 2014-09-24, Last modification date: 2023-11-15) |
| Primary citation | Chen, S.,Gopalakrishnan, R.,Schaer, T.,Marger, F.,Hovius, R.,Bertrand, D.,Pojer, F.,Heinis, C. Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides. Nat Chem, 6:1009-1016, 2014 Cited by PubMed Abstract: The disulfide bonds that form between two cysteine residues are important in defining and rigidifying the structures of proteins and peptides. In polypeptides containing multiple cysteine residues, disulfide isomerization can lead to multiple products with different biological activities. Here, we describe the development of a dithiol amino acid (Dtaa) that can form two disulfide bridges at a single amino acid site. Application of Dtaas to a serine protease inhibitor and a nicotinic acetylcholine receptor inhibitor that contain disulfide constraints enhanced their inhibitory activities 40- and 7.6-fold, respectively. X-ray crystallographic and NMR structure analysis show that the peptide ligands containing Dtaas have retained their native tertiary structures. We furthermore show that replacement of two cysteines by Dtaas can avoid the formation of disulfide bond isomers. With these properties, Dtaas are likely to have broad application in the rational design or directed evolution of peptides and proteins with high activity and stability. PubMed: 25343607DOI: 10.1038/nchem.2043 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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