Solution structures of the fibronectin-like Leishmania gp63 SRYD-containing sequence in the free and antibody-bound states - Transferred NOE and molecular dynamics studies
Φόρτωση...
Ημερομηνία
Συγγραφείς
Petit, M. C.
Orlewski, P.
Tsikaris, V.
Sakarellos-Daitsiotis, M.
Sakarellos, C.
Tzinia, A.
Konidou, G.
Soteriadou, K. P.
Marraud, M.
Cung, M. T.
Τίτλος Εφημερίδας
Περιοδικό ISSN
Τίτλος τόμου
Εκδότης
Springer-Verlag
Περίληψη
Τύπος
Είδος δημοσίευσης σε συνέδριο
Είδος περιοδικού
peer reviewed
Είδος εκπαιδευτικού υλικού
Όνομα συνεδρίου
Όνομα περιοδικού
European Journal of Biochemistry
Όνομα βιβλίου
Σειρά βιβλίου
Έκδοση βιβλίου
Συμπληρωματικός/δευτερεύων τίτλος
Περιγραφή
The anti-SRYD monoclonal antibody (mAbSRYD) raised against the IASRYDQL synthetic octapeptide, the 250-257 sequence of the Leishmania major surface glycoprotein gp63 recognizes both SRYD-containing peptides and the whole cognate major surface protein on intact parasites. Two SRYD-containing peptides. which antigenically and functionally mimic the RGDS sequence of fibronectin and efficiently inhibit parasite attachment to the macrophage receptors. were studied by two-dimensional transferred nuclear Overhauser effect experiments in the presence of mAbSRYD. The antibody-bound IASRYDQL octapeptide solution conformation was determined on the basis of 55 interproton-distance restraints, derived from NMR measurements. Eighteen structures which were first generated using an approach combining distance geometry and molecular dynamics, converge by energy minimization toward a folded structure with an average rmsd from the experimental data of less than 0.05 nm for the overall backbone and 0.025 nm for the SRYD motif. A distorted y-turn was found, stabilized by the backbone-backbone D255-NH to R253-CO hydrogen bond, while the R253 and D255 side chains are pointing in opposite directions. This latter antibody-bound structure is compared with that of the free octapeptide in dimethylsulfoxide solution, and with thr crystal structure of the RYD fragment in OPG2 Fab, an antireceptor antibody that mimics the RGD cell adhesion site. On this basis, a mechanism for IASRYDQL-receptor interaction is discussed.
Περιγραφή
Λέξεις-κλειδιά
antigen-antibody interaction, leishmania gp63, molecular dynamics, sryd motif, transferred noe, major surface glycoprotein, magnetic-resonance spectroscopy, monoclonal-antibody, cell-adhesion, cutaneous leishmaniasis, effective immunization, protective immunity, fibrinogen receptor, secondary structure, zinc-binding
Θεματική κατηγορία
Παραπομπή
Σύνδεσμος
<Go to ISI>://000073002500023
http://onlinelibrary.wiley.com/store/10.1046/j.1432-1327.1998.2530184.x/asset/j.1432-1327.1998.2530184.x.pdf?v=1&t=h0e0p1ra&s=7e6b1005887e4f49d9bb126bbc71d16710696f90
http://onlinelibrary.wiley.com/store/10.1046/j.1432-1327.1998.2530184.x/asset/j.1432-1327.1998.2530184.x.pdf?v=1&t=h0e0p1ra&s=7e6b1005887e4f49d9bb126bbc71d16710696f90
Γλώσσα
en
Εκδίδον τμήμα/τομέας
Όνομα επιβλέποντος
Εξεταστική επιτροπή
Γενική Περιγραφή / Σχόλια
Ίδρυμα και Σχολή/Τμήμα του υποβάλλοντος
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας