Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4942
Title: NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin
Authors: Bernini, Andrea 
Ciutti, A.
Spiga, Ottavia 
Scarselli, M.
Klein, S.
Vannetti, S.
Bracci, Luisa
Lozzi, Luisa
Lelli, Barbara
Falciani, Chiara
Neri, P.
Niccolai, Neri 
Issue Date: 2004
Project: None 
Journal: JOURNAL OF MOLECULAR BIOLOGY
Abstract: 
The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several methods and a wealth of functional, kinetic and structural data are available. Hence, this system represents a suitable model to explore in detail the dynamics of a peptide-protein interaction. Here, the solution structure of a new complex of the protein toxin with a tridecapeptide ligand exhibiting high affinity has been determined by NMR. As observed for three other previously reported mimotope-alpha-bungarotoxin complexes, also in this case correlations between biological activity and kinetic data are not fully consistent with a static discussion of structural data. Molecular dynamics simulations of the four mimotope-toxin complexes indicate that a relevant contribution to the complex stability is given by the extent of the residual flexibility that the protein maintains upon peptide binding. This feature, limiting the entropy loss caused by protein folding and binding, ought to be generally considered in a rational design of specific protein ligands.
Description: 
42524
URI: http://hdl.handle.net/20.500.12779/4942
ISSN: 0022-2836
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