The specificity of Av3 sea anemone toxin for arthropods is determined at linker DI/SS2–S6 in the pore module of target sodium channels

2014 ◽  
Vol 463 (2) ◽  
pp. 271-277 ◽  
Author(s):  
Maya Gur Barzilai ◽  
Roy Kahn ◽  
Noa Regev ◽  
Dalia Gordon ◽  
Yehu Moran ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Sodium Channels ◽  
Receptor Site ◽  
Sea Anemone ◽  
Sea Anemone Toxin

A sodium channel determinant that dictates the specificity of Av3 sea anemone toxin for arthropods was identified using channel-swapping experiments and mutagenesis. This finding provides a clue as to the receptor site of Av3 on the sodium channel.

Expression and Mutagenesis of the Sea Anemone Toxin Av2 Reveals Key Amino Acid Residues Important for Activity on Voltage-Gated Sodium Channels†

Biochemistry ◽  
2006 ◽  
Vol 45 (29) ◽  
pp. 8864-8873 ◽  
Author(s):  
Yehu Moran ◽  
Lior Cohen ◽  
Roy Kahn ◽  
Izhar Karbat ◽  
Dalia Gordon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sodium Channels ◽  
Sea Anemone ◽  
Amino Acid Residues ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Sea Anemone Toxin

scholarly journals Solution Structure and Alanine Scan of a Spider Toxin That Affects the Activation of Mammalian Voltage-gated Sodium Channels

2006 ◽  
Vol 282 (7) ◽  
pp. 4643-4652 ◽  
Author(s):  
Gerardo Corzo ◽  
Jennifer K. Sabo ◽  
Frank Bosmans ◽  
Bert Billen ◽  
Elba Villegas ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Sodium Channels ◽  
Solution Structure ◽  
Receptor Site ◽  
Amino Acid Sequences ◽  
Structural Motif ◽  
Dimensional Structure ◽  
Voltage Gated Sodium Channel ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels

Magi 5, from the hexathelid spider Macrothele gigas, is a 29-residue polypeptide containing three disulfide bridges. It binds specifically to receptor site 4 on mammalian voltage-gated sodium channels and competes with scorpion β-toxins, such as Css IV from Centruroides suffusus suffusus. As a consequence, Magi 5 shifts the activation voltage of the mammalian rNav1.2a channel to more hyperpolarized voltages, whereas the insect channel, DmNav1, is not affected. To gain insight into toxin-channel interactions, Magi 5 and 23 analogues were synthesized. The three-dimensional structure of Magi 5 in aqueous solution was determined, and its voltage-gated sodium channel-binding surfaces were mapped onto this structure using data from electrophysiological measurements on a series of Ala-substituted analogues. The structure clearly resembles the inhibitor cystine knot structural motif, although the triple-stranded β-sheet typically found in that motif is partially distorted in Magi 5. The interactive surface of Magi 5 toward voltage-gated sodium channels resembles in some respects the Janus-faced atracotoxins, with functionally important charged residues on one face of the toxin and hydrophobic residues on the other. Magi 5 also resembles the scorpion β-toxin Css IV, which has distinct nonpolar and charged surfaces that are critical for channel binding and has a key Glu involved in voltage sensor trapping. These two distinct classes of toxin, with different amino acid sequences and different structures, may utilize similar groups of residues on their surface to achieve the common end of modifying voltage-gated sodium channel function.

New Sea Anemone Toxin RTX-VI Selectively Modulates Voltage-Gated Sodium Channels

2020 ◽  
Vol 495 (1) ◽  
pp. 292-295
Author(s):  
R. S. Kalina ◽  
S. Peigneur ◽  
I. N. Gladkikh ◽  
P. S. Dmitrenok ◽  
N. Y. Kim ◽  
...  
Keyword(s):  
Sodium Channels ◽  
Sea Anemone ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Sea Anemone Toxin
Sign in / Sign up

Export Citation Format

Share Document