1TXA

SOLUTION NMR STRUCTURE OF TOXIN B, A LONG NEUROTOXIN FROM THE VENOM OF THE KING COBRA, MINIMIZED AVERAGE STRUCTURE

Summary for 1TXA

• Entry DOI: 10.2210/pdb1txa/pdb
• Descriptor: TOXIN B (1 entity in total)
• Functional Keywords: venom, neurotoxin, multigene family, toxin b
• Biological source: Ophiophagus hannah (king cobra)
• Cellular location: Secreted : P01386
• Total number of polymer chains: 1
• Total formula weight: 8065.25

Authors

Peng, S.-S.,Kumar, T.K.S.,Jayaraman, G.,Chang, C.-C.,Yu, C. (deposition date: 1996-07-20, release date: 1997-10-15, Last modification date: 2017-11-29)

Primary citation

Peng, S.S.,Kumar, T.K.,Jayaraman, G.,Chang, C.C.,Yu, C.
Solution structure of toxin b, a long neurotoxin from the venom of the king cobra (Ophiophagus hannah).
J.Biol.Chem., 272:7817-7823, 1997

PubMed Abstract: The solution structure of toxin b, a long neurotoxin (73 amino acids and 5 disulfides) from the venom of Ophiophagus hannah (king cobra), has been determined using 1H NMR and dynamical simulated annealing techniques. The structures were calculated using 485 distance constraints and 52 dihedral angle restraints. The 21 structures that were obtained satisfy the experimental restraints and possess good nonbonded contacts. Analysis of the converged structures revealed that the protein consists of a core region from which three finger-like loops extend outwards. The regular secondary structure in toxin b includes a double and a triple stranded antiparallel beta sheet. Comparison with the solution structures of other long neurotoxins reveals that although the structure of toxin b is similar to those of previously reported long neurotoxins, clear local structural differences are observed in regions proposed to be involved in binding to the acetylcholine receptor. A positively charged cluster is found in the C-terminal tail, in Loop III, and in the tip of Loop II. This cationic cluster could be crucial for the binding of the long neurotoxins to the acetylcholine receptor.

PubMed: 9065446
DOI: 10.1074/jbc.272.12.7817

Experimental method

SOLUTION NMR