1RGJ

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

Replaces:  1P67

Summary for 1RGJ

• Entry DOI: 10.2210/pdb1rgj/pdb
• Related: 1HOY 1IK8 1IKC 1JBD
• NMR Information: BMRB: 5988
• Descriptor: long neurotoxin 1, MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR (2 entities in total)
• Functional Keywords: neurotoxin, protein-peptide complex, alpha-bungarotoxin, beta-strands, toxin
• Biological source: Bungarus multicinctus (many-banded krait); More
• Cellular location: Secreted: P60615
• Total number of polymer chains: 2
• Total formula weight: 9713.05

Authors

Bernini, A.,Spiga, O.,Ciutti, A.,Scarselli, M.,Bracci, L.,Lozzi, L.,Lelli, B.,Neri, P.,Niccolai, N. (deposition date: 2003-11-12, release date: 2003-11-25, Last modification date: 2024-11-13)

Primary citation

Bernini, A.,Ciutti, A.,Spiga, O.,Scarselli, M.,Klein, S.,Vannetti, S.,Bracci, L.,Lozzi, L.,Lelli, B.,Falciani, C.,Neri, P.,Niccolai, N.
NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
J.Mol.Biol., 339:1169-1177, 2004

PubMed 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.

PubMed: 15178256
DOI: 10.1016/j.jmb.2004.04.041

Experimental method

SOLUTION NMR