1s4j
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(New page: 200px<br /> <applet load="1s4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s4j" /> '''NMR structure of cross-reactive peptides fr...)
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Revision as of 17:04, 12 November 2007
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NMR structure of cross-reactive peptides from Homo sapiens
Overview
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.
About this Structure
1S4J is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
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