Article
Functional mutation of multiple solvent-exposed loops in the Ecballium elaterium trypsin inhibitor-II cystine knot miniprotein.
PloS one - 18 Feb 2011
Kimura Richard H, Jones Douglas S, Jiang Lei, Miao Zheng, Cheng Zhen, Cochran Jennifer R
Abstract excerpt
BACKGROUND: The Ecballium elaterium trypsin inhibitor (EETI-II), a 28-amino acid member of the knottin family of peptides, contains three interwoven disulfide bonds that form multiple solvent-exposed loops. Previously, the trypsin binding loop of EETI-II has been engineered to confer binding to several alternative molecular targets. Here, EETI-II was further explored as a molecular scaffold for polypeptide...
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