The Ecballium elaterium trypsin inhibitor II (EETI-II) belongs to the family of squash inhibitors and is one of the strongest inhibitors known for trypsin. The eight independent molecules of EETI-II in the crystal structure reported here provide a good opportunity to test the hypothesis that this small cystine-knot protein (knottin) is sufficiently rigid to be used as a molecular scaffold for protein-engineering purposes. To extend this test, the structures of two complexes of EETI-II with trypsin have also been determined, one carrying a four-amino-acid mutation of EETI-II. The remarkable similarity of these structures confirms the rigidity of the molecular framework and hence its suitability as a molecular scaffold. © 2005 International Union of Crystallography - all rights reserved.
CITATION STYLE
Krätzner, R., Debreczeni, J. É., Pape, T., Schneider, T. R., Wentzel, A., Kolmar, H., … Uson, I. (2005). Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): A rigid molecular scaffold. Acta Crystallographica Section D: Biological Crystallography, 61(9), 1255–1262. https://doi.org/10.1107/S0907444905021207
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