TY - JOUR
T1 - Production of recombinant Conkunitzin-S1 in Escherichia coli
AU - Bayrhuber, Monika
AU - Graf, Roland
AU - Ferber, Michael
AU - Zweckstetter, Markus
AU - Imperial, Julita
AU - Garrett, James E.
AU - Olivera, Baldomero M.
AU - Terlau, Heinrich
AU - Becker, Stefan
PY - 2006/6/1
Y1 - 2006/6/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33646558307&partnerID=8YFLogxK
U2 - 10.1016/j.pep.2006.01.019
DO - 10.1016/j.pep.2006.01.019
M3 - Journal articles
C2 - 16542850
AN - SCOPUS:33646558307
SN - 1046-5928
VL - 47
SP - 640
EP - 644
JO - Protein Expression and Purification
JF - Protein Expression and Purification
IS - 2
ER -
