1S4J
NMR structure of cross-reactive peptides from Homo sapiens
Summary for 1S4J
| Entry DOI | 10.2210/pdb1s4j/pdb |
| Related | 1S4H |
| NMR Information | BMRB: 6106 |
| Descriptor | 60S acidic ribosomal protein P2 (1 entity in total) |
| Functional Keywords | antigenic peptide, ribosomal p2 protein, chagas disease, ribosome |
| Total number of polymer chains | 1 |
| Total formula weight | 1476.48 |
| Authors | Soares, M.R.,Bisch, P.M.,Campos de Carvalho, A.C.,Valente, A.P.,Almeida, F.C.L. (deposition date: 2004-01-16, release date: 2004-03-16, Last modification date: 2024-05-29) |
| Primary citation | Soares, M.R.,Bisch, P.M.,Campos De Carvalho, A.C.,Valente, A.P.,Almeida, F.C.L. Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis Febs Lett., 560:134-140, 2004 Cited by PubMed Abstract: The structure of peptides corresponding to the C-terminal residues from Trypanosoma cruzi (R13), human (H13) and Leishmania braziliensis (A13) ribosomal proteins were determined using nuclear magnetic resonance. Although there is only one amino acid difference between them, the peptides present distinct structures in solution: R13 adopts a random coil conformation while H13 and A13 form a bend. Interaction of these peptides with polyclonal antibodies from chronic Chagas' disease patients and a monoclonal antibody raised against T. cruzi ribosomal P2beta protein was probed by transferred NOE. The results show that the flexibility of R13 is fundamental for the binding to the antibody. PubMed: 14988012DOI: 10.1016/S0014-5793(04)00088-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
