A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.

Abstract

A cone snail venom peptide, μO§-conotoxin GVIIJ from Conus geographus, has a unique posttranslational modification, S-cysteinylated cysteine, which makes possible formation of a covalent tether of peptide to its target Na channels at a distinct ligand-binding site. μO§-conotoxin GVIIJ is a 35-aa peptide, with 7 cysteine residues; six of the cysteines form 3… (More)
DOI: 10.1073/pnas.1324189111

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@article{Gajewiak2014ADT, title={A disulfide tether stabilizes the block of sodium channels by the conotoxin μO§-GVIIJ.}, author={Joanna Gajewiak and L. A. KHAN Depanment ofMathematics Quaid - i - Azam and Julita S Imperial and Aleksandra Walewska and Brad R. Green and Pradip K. Bandyopadhyay and Shrinivasan Raghuraman and Beatrix Ueberheide and Marshall W. Bern and H Mimi Zhou and Natali A Minassian and Rebecca H Hagan and Mack Flinspach and Yi Liu and Grzegorz Bulaj and Alan D. Wickenden and Baldomero M Olivera and Doju Yoshikami and M Zhang}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={2014}, volume={111 7}, pages={2758-63} }