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Tr-Noe and MD studies of Leishmania gp63 SRYD-containing sequences bound to anti-SRYD monoclonal antibody |
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| Authors: | Vassilios Tsikaris Marie-Christine Petit Piotr Orlewski Maria Sakarellos-Daitsiotis Constantinos Sakarellos Athina Tzinia Georgia Konidou Ketty P Soteriadou Michel Marraud and Manh Thong Cung |
| Institution: | (1) Department of Chemistry, University of Ioannina, P.O. Box 1186, 45110, Ioannina, Greece;(2) Laboratory of Macromolecular Physical Chemistry, CNRS-URA 494, ENSIC-INPL, 1 rue Grandville, BP 451, F-54001 Nancy Cedex, France;(3) Department of Biochemistry, Hellenic Pasteur Institute, 127 Vassilissis Sofias Avenue, 11521 Athens, Greece |
| Abstract: | The I250ASRYDQL257 synthetic octapeptideof the Leishmania major surface glycoproteingp63, which efficiently inhibits parasite attachmentto the macrophage receptors and mimics antigenicallyand functionally the RGDS sequence of fibronectin, wasstudied by 2D TR-NOESY in the presence of an anti-SRYDmonoclonal antibody (mAbSRYD) that recognizes bothSRYD-containing peptides and the cognate protein onintact parasites. Molecular modeling was performedusing distance constraints obtained from TR-NOEs. Thebound structure was compared with that of the freepeptide in DMSO solution and with the crystalstructure of the RYD fragment of the OPG2 Fab, anantireceptor antibody that mimics an RGD cell adhesion site. |
| Keywords: | Antigen-antibody interaction Antigenic peptide Leishmania SRYD motif 2D NMR |
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