2cmy: Difference between revisions
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[[Image:2cmy. | [[Image:2cmy.jpg|left|200px]]<br /><applet load="2cmy" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2cmy" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="2cmy, resolution 2.25Å" /> | caption="2cmy, resolution 2.25Å" /> | ||
'''CRYSTAL COMPLEX BETWEEN BOVINE TRYPSIN AND VERONICA HEDERIFOLIA TRYPSIN INHIBITOR'''<br /> | '''CRYSTAL COMPLEX BETWEEN BOVINE TRYPSIN AND VERONICA HEDERIFOLIA TRYPSIN INHIBITOR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2CMY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Veronica_hederifolia Veronica hederifolia] with SO4, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | 2CMY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Veronica_hederifolia Veronica hederifolia] with SO4, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Known structural/functional Site: <scene name='pdbsite=CAT:Gol Binding Site For Chain A'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CMY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:29:27 2007'' | ||
Revision as of 20:19, 18 December 2007
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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. Unusually, the crystallised complex is in the form of a stabilised acyl-enzyme, intermediate with the scissile bond of the VhTI inhibitor cleaved and the, resulting N-terminal portion of the inhibitor remaining attached to the, trypsin catalytic serine 195 by an ester bond. A synthetic, truncated, version of the VhTI peptide has also been produced and co-crystallised, with trypsin but, surprisingly, is seen to be uncleaved and consequently, forms a non-covalent complex with trypsin. The VhTI peptide shows that, effective enzyme inhibitors can be constructed from simple helical motifs, and provides a new scaffold on which to base the design of novel serine, protease inhibitors.
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 Known structural/functional Site: . 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
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