2plx: Difference between revisions

Revision as of 21:10, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2plx.png

Template:STRUCTURE 2plx

Trypsin complexed to a synthetic peptide from Veronica hederifoliaTrypsin complexed to a synthetic peptide from Veronica hederifolia

Template:ABSTRACT PUBMED 17640870

About this StructureAbout this Structure

2PLX is a Single protein structure of sequence from Bos taurus. 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 J, Joseph-Horne T, Shewry P, Brady RL, J Biol Chem. 2007 Sep 21;282(38):27760-8. Epub 2007 Jul 19. PMID:17640870

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Trypsin complexed to a synthetic peptide from Veronica hederifolia'''
+===Trypsin complexed to a synthetic peptide from Veronica hederifolia===
-==Overview==
+<!--
-The storage tissues of many plants contain protease inhibitors that 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 submicromolar apparent K(i) 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 disulfide bonds. Unusually, the crystallized complex is in the form of a stabilized 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-crystallized with trypsin but, surprisingly, is seen to be uncleaved and consequently forms a noncovalent 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17640870}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17640870}}
 ==About this Structure==
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 [[Category: Helix-turn-helix]]
 [[Category: Hydrolase]]
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