2cmy
|
CRYSTAL COMPLEX BETWEEN BOVINE TRYPSIN AND VERONICA HEDERIFOLIA TRYPSIN INHIBITOR
OverviewOverview
The storage tissues of many plants contain protease inhibitors which are, believed to play an important role in defending the plant from invasion by, pests and pathogens. These proteinaceous inhibitor molecules belong to a, number of structurally distinct families. We describe here the isolation, purification, initial inhibitory properties and three dimensional, structure of a novel trypsin inhibitor from seeds of Veronica hederifolia, (VhTI). The VhTI peptide inhibits trypsin with a sub-micromolar apparent, Ki, and is expected to be specific for trypsin-like serine proteases. VhTI, differs dramatically in structure from all previously-described families, of trypsin inhibitors, consisting of a helix-turn-helix motif, with the, two alpha helices tightly associated by two disulphide bonds. ... [(full description)]
About this StructureAbout this Structure
2CMY is a [Protein complex] structure of sequences from [Bos taurus] and [Veronica hederifolia] with SO4, CA and GOL as [ligands]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
ReferenceReference
An unusual helix-turn-helix protease inhibitory motif in a novel trypsin inhibitor from seeds of veronica (Veronica hederifolia L.)., Conners R, Konarev AV, Forsyth J, Lovegrove A, Marsh JT, Joseph-Horne T, Shewry P, Brady RL, J Biol Chem. 2007 Jul 19;. PMID:17640870
Page seeded by OCA on Tue Oct 30 13:07:52 2007