1JBD

NMR Structure of the Complex Between alpha-bungarotoxin and a Mimotope of the Nicotinic Acetylcholine Receptor

Replaces:  1HN7

Summary for 1JBD

• Entry DOI: 10.2210/pdb1jbd/pdb
• Related: 1HN7 1HOY 1IK8 1IKC
• NMR Information: BMRB: 5006
• Descriptor: LONG NEUROTOXIN 1, MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR (2 entities in total)
• Functional Keywords: alpha-bungarotoxin, protein-peptide complex, achr, toxin
• Biological source: Bungarus multicinctus (many-banded krait); More
• Cellular location: Secreted: P60615
• Total number of polymer chains: 2
• Total formula weight: 9849.23

Authors

Scarselli, M.,Spiga, O.,Ciutti, A.,Bracci, L.,Lelli, B.,Lozzi, L.,Calamandrei, D.,Bernini, A.,Di Maro, D.,Klein, S.,Niccolai, N. (deposition date: 2001-06-04, release date: 2001-06-27, Last modification date: 2024-10-16)

Primary citation

Scarselli, M.,Spiga, O.,Ciutti, A.,Bernini, A.,Bracci, L.,Lelli, B.,Lozzi, L.,Calamandrei, D.,Di Maro, D.,Klein, S.,Niccolai, N.
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Biochemistry, 41:1457-1463, 2002

PubMed Abstract: A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the sequences, which inhibited binding of alpha-bungarotoxin to muscle and neuronal nicotinic receptors, HRYYESSLPWYPD, a 14-amino acid peptide with considerably higher toxin-binding affinity than the other synthesized peptides, was selected, and the structure of its complex with the toxin was analyzed by NMR. Comparison of the solution structure of the free toxin and its complex with this peptide indicated that complex formation induced extensive conformational rearrangements mainly at finger II and the carboxy terminus of the protein. The peptidyl residues P10 and Y4 seemed to be critical for peptide folding and complex stability, respectively. The latter residue of the peptide strongly interacted with the protein by entering a small pocket delimited by D30, C33, S34, R36, and V39 toxin side chains.

PubMed: 11814338
DOI: 10.1021/bi011012f

Experimental method

SOLUTION NMR