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          Institute: MPI für experimentelle Medizin     Collection: MCN     Display Documents



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ID: 292179.0, MPI für experimentelle Medizin / MCN
Production of recombinant Conkunitzin-S1 in Escherichia coli
Authors:Bayrhuber, Monika; Graf, Roland; Ferber, Michael; Zweckstetter, Markus; Imperial, Julita; Garrett, James E.; Olivera, Baldomero M.; Terlau, Heinrich; Becker, Stefan
Language:English
Date of Publication (YYYY-MM-DD):2006-06
Title of Journal:Protein Expression and Purification
Journal Abbrev.:Protein Expression and Purification
Volume:47
Issue / Number:2
Start Page:640
End Page:644
Review Status:Peer-review
Audience:Experts Only
Abstract / Description: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.
Free Keywords:Conkunitzin-S1; Kunitz domain fold; cone snail; potassium channel PROTEINS; INTEIN; EXPRESSION; PEPTIDES; CLEAVAGE; CHANNEL; SYSTEM
External Publication Status:published
Document Type:Article
Communicated by:Heinrich Terlau
Affiliations:MPI für experimentelle Medizin/MCN
Identifiers:ISSN:1046-5928 [ID No:1]
ISI:000238277000038 [ID No:2]
ISI:000238277000038 [ID No:3]
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