English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Production of recombinant Conkunitzin-S1 in Escherichia coli

MPS-Authors
/persons/resource/persons182147

Ferber,  Michael
Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society;

/persons/resource/persons15918

Terlau,  Heinrich
Molecular and cellular neuropharmacology, Max Planck Institute of Experimental Medicine, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Bayrhuber, M., Graf, R., Ferber, M., Zweckstetter, M., Imperial, J., Garrett, J. E., et al. (2006). Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expression and Purification, 47(2), 640-644.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-24DE-F
Abstract
Conkunitzin-S1 from the cone snail Conus striatus is the first member of a new neurotoxin family with a canonical Kunitz domain fold. Conk-SI is 60 amino acids long and lacks one of the three conserved disulfide bonds typically found in Kunitz domain modules. It binds specifically to voltage activated potassium channels of the Shaker family. The peptide was expressed in insoluble form in fusion with an N-terminal intein. Refolding in the presence of glutathione followed by pH shift-induced cleavage of the fusion protein resulted in a functional toxin as demonstrated by voltage-clamp measurements. (c) 2006 Elsevier Inc. All rights reserved.