1PBZ
DE NOVO DESIGNED PEPTIDE-METALLOPORPHYRIN COMPLEX, SOLUTION STRUCTURE
Summary for 1PBZ
| Entry DOI | 10.2210/pdb1pbz/pdb |
| Descriptor | De novo designed cyclic peptide, COPROPORPHYRIN I CONTAINING CO(III) (2 entities in total) |
| Functional Keywords | peptide; metalloporphyrin; heme; de novo design, de novo protein |
| Total number of polymer chains | 2 |
| Total formula weight | 3883.24 |
| Authors | Wang, J.,Rosenblatt, M.M.,Suslick, K.S. (deposition date: 2003-05-15, release date: 2003-12-09, Last modification date: 2024-11-06) |
| Primary citation | Rosenblatt, M.M.,Wang, J.,Suslick, K.S. De novo designed cyclic-peptide heme complexes Proc.Natl.Acad.Sci.USA, 100:13140-13145, 2003 Cited by PubMed Abstract: The structural characterization of de novo designed metalloproteins together with determination of chemical reactivity can provide a detailed understanding of the relationship between protein structure and functional properties. Toward this goal, we have prepared a series of cyclic peptides that bind to water-soluble metalloporphyrins (FeIII and CoIII). Neutral and positively charged histidine-containing peptides bind with a high affinity, whereas anionic peptides bind only weakly to the negatively charged metalloporphyrin. Additionally, it was found that the peptide becomes helical only in the presence of the metalloporphyrin. CD experiments confirm that the metalloporphyrin binds specific cyclic peptides with high affinity and with isodichroic behavior. Thermal unfolding experiments show that the complex has "native-like" properties. Finally, NMR spectroscopy produced well dispersed spectra and experimental restraints that provide a high-resolution solution structure of the complexed peptide. PubMed: 14595023DOI: 10.1073/pnas.2231273100 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
