1HC9

alpha-bungarotoxin complexed with high affinity peptide

Summary for 1HC9

• Entry DOI: 10.2210/pdb1hc9/pdb
• Related: 1ABT 1BXP 1HAA 1HAJ 1HN7 1HOY 1IDG 1IDH 1IDI 1IDL 2BTX
• Descriptor: ALPHA-BUNGAROTOXIN ISOFORM V31, ALPHA-BUNGAROTOXIN ISOFORM A31, PEPTIDE INHIBITOR, ... (5 entities in total)
• Functional Keywords: toxin/peptide, complex (toxin-peptide), acetylcholine receptor mimitope, alpha-bungarotoxin, 3- finger, protein-peptide complex, toxin, toxin-peptide complex
• Biological source: BUNGARUS MULTICINCTUS (MANY-BANDED KRAIT); More
• Cellular location: Secreted : P60616 P60615
• Total number of polymer chains: 4
• Total formula weight: 19672.11

Authors

Harel, M.,Kasher, R.,Sussman, J.L. (deposition date: 2001-05-02, release date: 2001-11-10, Last modification date: 2024-10-16)

Primary citation

Harel, M.,Kasher, R.,Nicolas, A.,Guss, J.M.,Balass, M.,Fridkin, M.,Smit, A.B.,Brejc, K.,Sixma, T.K.,Katchalski-Katzir, E.,Sussman, J.L.,Fuchs, S.
The Binding Site of Acetylcholine Receptor as Visualized in the X-Ray Structure of a Complex between Alpha-Bungarotoxin and a Mimotope Peptide.
Neuron, 32:265-, 2001

PubMed Abstract: We have determined the crystal structure at 1.8 A resolution of a complex of alpha-bungarotoxin with a high affinity 13-residue peptide that is homologous to the binding region of the alpha subunit of acetylcholine receptor. The peptide fits snugly to the toxin and adopts a beta hairpin conformation. The structures of the bound peptide and the homologous loop of acetylcholine binding protein, a soluble analog of the extracellular domain of acetylcholine receptor, are remarkably similar. Their superposition indicates that the toxin wraps around the receptor binding site loop, and in addition, binds tightly at the interface of two of the receptor subunits where it inserts a finger into the ligand binding site, thus blocking access to the acetylcholine binding site and explaining its strong antagonistic activity.

PubMed: 11683996
DOI: 10.1016/S0896-6273(01)00461-5

Experimental method

X-RAY DIFFRACTION (1.8 Å)