1IKC
NMR Structure of alpha-Bungarotoxin
Summary for 1IKC
| Entry DOI | 10.2210/pdb1ikc/pdb |
| Related | 1HN7 1HOY 1IK8 |
| Descriptor | long neurotoxin 1 (1 entity in total) |
| Functional Keywords | alpha-bungarotoxin, toxin, nicotinic-acetilcholine receptor |
| Biological source | Bungarus multicinctus (many-banded krait) |
| Cellular location | Secreted: P60615 |
| Total number of polymer chains | 1 |
| Total formula weight | 8005.28 |
| Authors | Niccolai, N.,Spiga, O.,Ciutti, A. (deposition date: 2001-05-03, release date: 2001-05-16, Last modification date: 2024-10-30) |
| 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 Cited by 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: 11814338DOI: 10.1021/bi011012f PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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