1s4j
From Proteopedia
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| - | [[Image:1s4j.gif|left|200px]] | ||
| - | + | ==NMR structure of cross-reactive peptides from Homo sapiens== | |
| - | + | <StructureSection load='1s4j' size='340' side='right'caption='[[1s4j]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1s4j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4J FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4j OCA], [https://pdbe.org/1s4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4j RCSB], [https://www.ebi.ac.uk/pdbsum/1s4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4j ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/RLA2_HUMAN RLA2_HUMAN] Plays an important role in the elongation step of protein synthesis.[HAMAP-Rule:MF_01478] | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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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. | 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<ref>PMID:14988012</ref> | |
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| - | 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 | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1s4j" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Almeida FCL]] | ||
| + | [[Category: Bisch PM]] | ||
| + | [[Category: Campos de Carvalho AC]] | ||
| + | [[Category: Soares MR]] | ||
| + | [[Category: Valente AP]] | ||
Current revision
NMR structure of cross-reactive peptides from Homo sapiens
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