Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Crystal structure of the complex between porcine beta-trypsin and the second domain of the Kazal-type ovomucoid turkey egg white trypsin inhibitor (OMTKY2) has been determined at 1.9A resolution. A peptide fragment from the first domain has been crystallized with the complex. Restrained-refinement of the structure led to an R-factor of 0.19 for the 32206 reflections. OMTKY2 exhibits the canonical Kazal-type fold with a central alpha-helix and a short two-stranded anti-parallel beta-sheet. The carbonyl carbon of the reactive site prefers trigonal geometry. The reactive site loop geometry of the inhibitor is complementary to the surface and charge of the binding site in beta-trypsin.
Crystal structure of trypsin-turkey egg white inhibitor complex.,Ibrahim BS, Pattabhi V Biochem Biophys Res Commun. 2004 Jan 2;313(1):8-16. PMID:14672690[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ibrahim BS, Pattabhi V. Crystal structure of trypsin-turkey egg white inhibitor complex. Biochem Biophys Res Commun. 2004 Jan 2;313(1):8-16. PMID:14672690
