Tr-Noe and MD studies of Leishmania gp63 SRYD-containing sequences bound to anti-SRYD monoclonal antibody View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-12

AUTHORS

Vassilios Tsikaris, Marie-Christine Petit, Piotr Orlewski, Maria Sakarellos-Daitsiotis, Constantinos Sakarellos, Athina Tzinia, Georgia Konidou, Ketty P. Soteriadou, Michel Marraud, Manh Thong Cung

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. More... »

PAGES

323-330

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1008896821140

DOI

http://dx.doi.org/10.1023/a:1008896821140

DIMENSIONS

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