1H9I

COMPLEX OF EETI-II MUTANT WITH PORCINE TRYPSIN

Summary for 1H9I

• Entry DOI: 10.2210/pdb1h9i/pdb
• Related: 1AKS 1AN1 1AVW 1AVX 1C9P 1EJA 1EPT 1EWU 1FMG 1FN6 1FNI 1H9H 1LDT 1MCT 1QQU 1TFX 2ETI 2LET
• Descriptor: TRYPSIN, TRYPSIN INHIBITOR II, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase/inhibitor, complex (serine protease-inhibitor), trypsin, squash inhibitor, cystine knot, hydrolase-inhibitor complex
• Biological source: SUS SCROFA (PIG); More
• Total number of polymer chains: 2
• Total formula weight: 27569.24

Authors

Kraetzner, R.,Wentzel, A.,Kolmar, H.,Uson, I. (deposition date: 2001-03-12, release date: 2004-07-26, Last modification date: 2024-10-16)

Primary citation

Kraetzner, R.,Debreczeni, J.E.,Pape, T.,Schneider, T.R.,Wentzel, A.,Kolmar, H.,Sheldrick, G.M.,Uson, I.
Structure of Ecballium Elaterium Trypsin Inhibitor II (Eeti-II): A Rigid Molecular Scaffold
Acta Crystallogr.,Sect.D, 61:1255-, 2005

PubMed Abstract: 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.

PubMed: 16131759
DOI: 10.1107/S0907444905021207

Experimental method

X-RAY DIFFRACTION (1.9 Å)