Summary
The I250 ASRYDQL257 synthetic octapeptide of theLeishmania major surface glycoprotein gp63, which efficiently inhibits parasite attachment to the macrophage receptors and mimics antigenically and functionally the RGDS sequence of fibronectin, was studied by 2D TR-NOESY in the presence of an anti-SRYD monoclonal antibody (mAbSRYD) that recognizes both SRYD-containing peptides and the cognate protein on intact parasites. Molecular modeling was performed using distance constraints obtained from TR-NOEs. The bound structure was compared with that of the free peptide in DMSO solution and with the crystal structure of the RYD fragment of the OPG2 Fab, an antireceptor antibody that mimics an RGD cell adhesion site.
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Tsikaris, V., Petit, MC., Orlewski, P. et al. TR-NOE and MD studies ofLeishmania gp63 SRYD-containing sequences bound to anti-SRYD monoclonal antibody. Lett Pept Sci 4, 323–330 (1997). https://doi.org/10.1007/BF02442896
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DOI: https://doi.org/10.1007/BF02442896