1s4h

NMR structure of cross-reactive peptides from L. braziliensisNMR structure of cross-reactive peptides from L. braziliensis

Structural highlights 1s4h is a 1 chain structure with sequence from Leishmania braziliensis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1s4h Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image