1h9i
From Proteopedia
COMPLEX OF EETI-II MUTANT WITH PORCINE TRYPSIN
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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 AlsoReferences
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