Please use this identifier to cite or link to this item:
|Title:||NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin||Authors:||Bernini, Andrea
|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.
|Appears in Collections:||Publications|
Show full item record
checked on May 17, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.