Next Article in Journal
Natural Occurrence of 2′,5′-Linked Heteronucleotides in Marine Sponges
Next Article in Special Issue
Behavioral and Chemical Ecology of Marine Organisms with Respect to Tetrodotoxin
Previous Article in Journal
Agarase: Review of Major Sources, Categories, Purification Method, Enzyme Characteristics and Applications
Mar. Drugs 2010, 8(2), 219-234; doi:10.3390/md8020219
Review

The Tetrodotoxin Binding Site Is within the Outer Vestibule of the Sodium Channel

*  and
Received: 23 December 2009 / Revised: 10 January 2010 / Accepted: 28 January 2010 / Published: 1 February 2010
(This article belongs to the Special Issue Tetrodotoxin)
View Full-Text   |   Download PDF [426 KB, uploaded 24 February 2015]   |   Browse Figures

Abstract

Tetrodotoxin and saxitoxin are small, compact asymmetrical marine toxins that block voltage-gated Na channels with high affinity and specificity. They enter the channel pore’s outer vestibule and bind to multiple residues that control permeation. Radiolabeled toxins were key contributors to channel protein purification and subsequent cloning. They also helped identify critical structural elements called P loops. Spacial organization of their mutation-identified interaction sites in molecular models has generated a molecular image of the TTX binding site in the outer vestibule and the critical permeation and selectivity features of this region. One site in the channel’s domain I P loop determines affinity differences in mammalian isoforms.
Keywords: marine toxins; Na channels; molecular modeling marine toxins; Na channels; molecular modeling
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
EndNote
MDPI and ACS Style

Fozzard, H.A.; Lipkind, G.M. The Tetrodotoxin Binding Site Is within the Outer Vestibule of the Sodium Channel. Mar. Drugs 2010, 8, 219-234.

View more citation formats

Related Articles

Article Metrics

For more information on the journal, click here

Comments

Cited By

[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert