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Primary structure of ammodytoxin C further reveals the toxic site of ammodytoxin.

作者信息

Krizaj I, Turk D, Ritonja A, Gubensek F

机构信息

Department of Biochemistry, J. Stefan Institute, Ljubljana, Yugoslavia.

出版信息

Biochim Biophys Acta. 1989 Nov 30;999(2):198-202. doi: 10.1016/0167-4838(89)90218-5.

Abstract

The sequence of ammodytoxin C, a presynaptically toxic, basic phospholipase A2 of Vipera ammodytes ammodytes venom was determined. The toxin differs only in two amino acid residues from the most toxic isotoxin ammodytoxin A and is 18-times less lethal. Ammodytoxin B which is 30-times less lethal than ammodytoxin A differs from it only in three amino acid residues. From the three-dimensional model of ammodytoxin A, it can be seen that mutated regions of ammodytoxin B and ammodytoxin C are on the surface, and relatively distant from each other. The observed decrease in toxicity of ammodytoxin C could be a consequence of changed charge in position 128 where a Lys is exchanged for Glu. The resulting change in electrostatic properties of the molecule which influences the orientation of the molecule during the approach to the charged nerve-terminal membrane might be responsible for the observed decrease in toxicity.

摘要

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