In-silico Structural and Functional Characterization of ?-bungarotoxin

- bungarotoxin (-BTX) is a bungarotoxins, contains the venom of the elapid snake Taiwanese banded krait (Bungarus multicinctus). It is a neurotoxin protein contains 74 amino acids having 8 kd with five disulphide bridges, that bind competitively to the nicotinic acetylcholine receptor found at the neuromuscular junction leads to cause paralysis, respiratory failure and death in the victim. nAChRs contain two binding sites for snake venom neurotoxins. The dynamics of binding action of these sites has proved difficult, although recent studies using normal mode dynamics have aided in predicting the nature of both the binding mechanisms of snake toxins and of ACh to nAChRs. A twist-like gating motion responsible for nAChR channel opening leads to increase diameter of channel with increase in motion, although neither the twist nor the increase in channel diameter was observed when the nAChR was in complex with either one or two -bungarotoxin molecules. The present study involves the study of physicochemical properties, secondary and tertiary structure prediction, study of nature of protein and its antigenicity by using bioinformatics tools. The in-silico study of this protein may revile the benefits of this protein in various ways.