Structural highlights
Function
[RLA2_LEIBR] Plays an important role in the elongation step of protein synthesis (By similarity).
Publication Abstract from PubMed
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.
Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis.,Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC FEBS Lett. 2004 Feb 27;560(1-3):134-40. PMID:14988012[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC. Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis. FEBS Lett. 2004 Feb 27;560(1-3):134-40. PMID:14988012 doi:10.1016/S0014-5793(04)00088-2
