1RGJ: NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN AND MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR WITH ENHANCED ACTIVITY

Citation:
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.
PDB ID: 1RGJDownload
MMDB ID: 25478
PDB Deposition Date: 2003/11/12
Updated in MMDB: 2003/12
Experimental Method:
solution nmr
Source Organism:
Bungarus multicinctus
Similar Structures:
Molecular Components in 1RGJ
Label Count Molecule
Proteins (2 molecules)
1
Long Neurotoxin 1
Molecule annotation
1
Mimotope of the Nicotinic Acetylcholine Receptor
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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