Article
Structure-activity relationship study of a scorpion toxin with high affinity for apamin-sensitive potassium channels by means of the solution structure of analogues.
International journal of peptide and protein research - 1 May 1995
Inisan A G, Meunier S, Fedelli O, Altbach M, Fremont V, Sabatier J M, Thévan A, Bernassau J M, Cambillau C, Darbon H
Abstract excerpt
Scorpion venoms contain numerous toxic polypeptides displaying various pharmacological activities. These toxins interact with ion channels of excitable membranes. Long toxins (60-70 amino acids) are known to interact with sodium channels, whereas most of the short toxins (31-37 amino acids) found their toxicity in modifying the potassium channel functions. A family of short scorpion toxins are known to interact...
Topics
- Amino Acid Sequence
- Animals
- Apamin
- Computer Simulation
- Molecular Sequence Data
- Mutation
- Potassium Channels
- Scorpion Venoms
- Software
- Structure-Activity Relationship