Production of recombinant Conkunitzin-S1 in Escherichia coli.

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-S1 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.

journal_name

Protein Expr Purif

authors

Bayrhuber M,Graf R,Ferber M,Zweckstetter M,Imperial J,Garrett JE,Olivera BM,Terlau H,Becker S

doi

10.1016/j.pep.2006.01.019

keywords:

subject

Has Abstract

pub_date

2006-06-01 00:00:00

pages

640-4

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(06)00039-8

journal_volume

47

pub_type

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