Structural highlights
Function
ITR2_ECBEL Inhibits trypsin.
Publication Abstract from PubMed
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.
Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold.,Kratzner R, Debreczeni JE, Pape T, Schneider TR, Wentzel A, Kolmar H, Sheldrick GM, Uson I Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1255-62. Epub 2005, Aug 16. PMID:16131759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kratzner R, Debreczeni JE, Pape T, Schneider TR, Wentzel A, Kolmar H, Sheldrick GM, Uson I. Structure of Ecballium elaterium trypsin inhibitor II (EETI-II): a rigid molecular scaffold. Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1255-62. Epub 2005, Aug 16. PMID:16131759 doi:http://dx.doi.org/10.1107/S0907444905021207