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Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): A rigid molecular scaffold

AutorKrätzner, Ralph; Debreczeny, Judith E.; Pape, Thomas; Schneider, Thomas R.; Wentzel, Alexander; Kolmar, Harald; Sheldrick, George M.; Usón, Isabel
Palabras claveknottins
inhibitors
EETI-II
molecular scaffolds
cystine knots
Fecha de publicaciónsep-2005
EditorBlackwell Publishing
CitaciónActa Crystallographica Section D: Biological Crystallography 61(9): 1255-1262 (2005)
ResumenThe 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.
Versión del editorhttp://dx.doi.org/10.1107/S0907444905021207
URIhttp://hdl.handle.net/10261/113909
DOI10.1107/S0907444905021207
Identificadoresdoi: 10.1107/S0907444905021207
issn: 0907-4449
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