TR-NOE and MD studies of Leishmania gp63 SRYD-containing sequences bound to anti-SRYD monoclonal antibody (Journal article)

Tsikaris, V./ Petit, M. C./ Orlewski, P./ Sakarellos-Daitsiotis, M./ Sakarellos, C./ Tzinia, A./ Konidou, G./ Soteriadou, K. P./ Marraud, M./ Cung, M. T.

The I(250)ASRYDQL(257) synthetic octapeptide of the Leishmania 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 Feb, an antireceptor antibody that mimics an RGD cell adhesion site.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: antigen-antibody interaction,antigenic peptide,leishmania gp63,molecular dynamics,sryd motif,2d nmr,major surface glycoprotein,protease gp63,cell-adhesion,promastigotes,spectroscopy,fibronectin,region,mimics,site
ISSN: 0929-5666
Link: <Go to ISI>://000071627900023
Publisher: Kluwer Academic Publishers
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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