2plx: Difference between revisions

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-[[Image:2plx.jpg|left|200px]]<br /><applet load="2plx" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2plx, resolution 1.560&Aring;" />
-'''Trypsin complexed to a synthetic peptide from Veronica hederifolia'''<br />
-==Overview==
+==Trypsin complexed to a synthetic peptide from Veronica hederifolia==
-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.
+<StructureSection load='2plx' size='340' side='right'caption='[[2plx]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2plx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Veronica_hederifolia Veronica hederifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PLX FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2plx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2plx OCA], [https://pdbe.org/2plx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2plx RCSB], [https://www.ebi.ac.uk/pdbsum/2plx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2plx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/2plx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2plx ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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<ref>PMID:17640870</ref>
-PLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=FLC:'>FLC</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PLX OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17640870 17640870]
+</div>
+<div class="pdbe-citations 2plx" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Trypsin 3D structures|Trypsin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Brady, R.L.]]
+[[Category: Veronica hederifolia]]
-[[Category: Conners, R.]]
+[[Category: Brady RL]]
-[[Category: CA]]
+[[Category: Conners R]]
-[[Category: FLC]]
-[[Category: GOL]]
-[[Category: helix-turn-helix]]
-[[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:56:57 2008''