Publication Type |
Journal Article |
School or College |
College of Science |
Department |
Biology |
Creator |
Olivera, Baldomero M. |
Other Author |
Jacobsen, Richard B.; Koch, E. Dietland; Lange-Malecki, Bettina; Stocker, Martin; Verhey, Janko; Van Wagoner, Ryan M.; Vyazovkina, Alexandra; Terlau, Heinrich |
Title |
Single amino acid substitutions in ĸ-conotoxin PVIIA disrupt interaction with the Shaker K+ channel |
Date |
2000 |
Description |
ĸ-Conotoxin PVIIA (ĸ-PVIIA), a 27-amino acid peptide with three disulfide cross-links, isolated from the venom of Conus purpurascens, is the first conopeptide shown to inhibit the Shaker K1 channel (Terlau, H., Shon, K., Grilley, M., Stocker, M., Stühmer, W., and Olivera, B. M. (1996) Nature 381, 148-151). Recently, two groups independently determined the solution structure for ĸ-PVIIA using NMR; although the structures reported were similar, two mutually exclusive models for the interaction of the peptide with the Shaker channel were proposed. |
Type |
Text |
Publisher |
American Society for Biochemistry and Molecular Biology (ASBMB) |
Volume |
275 |
Issue |
32 |
First Page |
24639 |
Last Page |
24644 |
Subject |
Conotoxins; k-conotoxin PVIIA; Shaker K+ channels; Conus purpurascens |
Subject LCSH |
Conus; Marine toxins |
Language |
eng |
Bibliographic Citation |
Jacobsen, R. B., Koch, E. D., Lange-Malecki, B., Stocker, M., Verhey, J., Van Wagoner, R. M., Vyazovkina, A., Olivera, B. M., & Terlau, H. (2000). Single amino acid substitutions in ĸ-conotoxin PVIIA disrupt interaction with the Shaker K+ channel. Journal of Biological Chemistry, 275(32), 24639-44. |
Rights Management |
(c)American Society for Biochemistry and Molecular Biology (ASBMB) http://www.asbmb.org/ |
Format Medium |
application/pdf |
Format Extent |
564,004 bytes |
Identifier |
ir-main,8395 |
ARK |
ark:/87278/s6bc4gtg |
Setname |
ir_uspace |
ID |
704140 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6bc4gtg |