2MTM
NMR structure of RCB-1 peptide
Summary for 2MTM
| Entry DOI | 10.2210/pdb2mtm/pdb |
| NMR Information | BMRB: 25169 |
| Descriptor | Putative uncharacterized protein (1 entity in total) |
| Functional Keywords | biomarker, natural product, unknown function |
| Biological source | Ricinus communis (Castor bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 2073.63 |
| Authors | Boldbaatar, D.,Elseedi, H.R. (deposition date: 2014-08-21, release date: 2015-09-02, Last modification date: 2024-11-06) |
| Primary citation | Boldbaatar, D.,Gunasekera, S.,El-Seedi, H.R.,Goransson, U. Synthesis, Structural Characterization, and Bioactivity of the Stable Peptide RCB-1 from Ricinus communis. J Nat Prod, 78:2545-2551, 2015 Cited by PubMed Abstract: The Ricinus communis biomarker peptides RCB-1 to -3 comprise homologous sequences of 19 (RCB-1) or 18 (RCB-2 and -3) amino acid residues. They all include four cysteine moieties, which form two disulfide bonds. However, neither the 3D structure nor the biological activity of any of these peptides is known. The synthesis of RCB-1, using microwave-assisted, Fmoc-based solid-phase peptide synthesis, and a method for its oxidative folding are reported. The tertiary structure of RCB-1, subsequently established using solution-state NMR, reveals a twisted loop fold with antiparallel β-sheets reinforced by the two disulfide bonds. Moreover, RCB-1 was tested for antibacterial, antifungal, and cytotoxic activity, as well as in a serum stability assay, in which it proved to be remarkably stable. PubMed: 26509914DOI: 10.1021/acs.jnatprod.5b00463 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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