On the molecular mechanism of action of scorpion neurotoxin: II. From Androctonus australis hector

✍ Scribed by J.R. Smythies; F. Benington; R.J. Bradley; W.F. Bridgers; R.D. Morin

• Book ID: 104155205
• Publisher: Elsevier Science
• Year: 1974
• Tongue: English
• Weight: 770 KB
• Volume: 43
• Category: Article
• ISSN: 0022-5193
• DOI: 10.1016/s0022-5193(74)80045-7

✦ Synopsis

An hypothesis has been presented earlier based on binding experiments that the ACh storage and release mechanism in the cholinergic terminal is based on a stack of CMP molecules. Such a stack can bind ACh in a 1 : 1 ratio and the resulting ACh-CMP complex is stereochemically complementary to morphine (1 : 1 • 1) and related drugs. The amino acid sequence of scorpion neurotoxin II (Androctonus australis Hector) has recently been published. This paper presents a model of the conformation of this protein, including its pattern of disulphide bond formation, that is to a high degree complementary to a stack of nine molecules of CMP. The conformation of the protein is predicted at two levels of confidence: (1) high (amino acids 48-64) and ( ) tentative (amino acids 1-47). If this theoretical conformation is confirmed by direct biophysical studies this will provide evidence in favour of the CMP hypothesis.