3std: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3std]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_grisea Pyricularia grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3STD FirstGlance]. <br>
<table><tr><td colspan='2'>[[3std]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_grisea Pyricularia grisea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3STD FirstGlance]. <br>
</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=MQ0:(3-AMINOMETHYL-CINNOLIN-4-YL)-(3,3-DIPHENYL-ALLYLIDENE)-AMINE'>MQ0</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#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=MQ0:(3-AMINOMETHYL-CINNOLIN-4-YL)-(3,3-DIPHENYL-ALLYLIDENE)-AMINE'>MQ0</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=3std FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3std OCA], [https://pdbe.org/3std PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3std RCSB], [https://www.ebi.ac.uk/pdbsum/3std PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3std ProSAT]</span></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=3std FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3std OCA], [https://pdbe.org/3std PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3std RCSB], [https://www.ebi.ac.uk/pdbsum/3std PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3std ProSAT]</span></td></tr>
</table>
</table>
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</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=3std ConSurf].
</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=3std ConSurf].
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== Publication Abstract from PubMed ==
Scytalone dehydratase (SD) is a molecular target of inhibitor design efforts aimed at protecting rice plants from the fungal disease caused by Magnaporthe grisea. As determined from X-ray diffraction data of an SD-inhibitor complex [Lundqvist et al. (1994) Structure (London) 2, 937-944], there is an extended hydrogen-bonding network between protein side chains, the inhibitor, and two bound water molecules. From models of SD complexed to quinazoline and benztriazine inhibitors, a new class of potent SD inhibitors involving the displacement of an active-site water molecule were designed. We were able to increase inhibitory potency by synthesizing compounds with a nitrile functionality displayed into the space occupied by one of the crystallographic water molecules. Sixteen inhibitors are compared. The net conversion of potent quinazoline and benztriazine inhibitors to cyanoquinolines and cyanocinnolines increased binding potency 2-20-fold. Replacement of the nitrile with a hydrogen atom lowered binding affinity 100-30,000-fold. X-ray crystallographic data at 1.65 A resolution on a SD-inhibitor complex confirmed that the nitrile functionality displaced the water molecule as intended and that a favorable orientation was created with tyrosines 30 and 50 which had been part of the hydrogen-bonding network with the water molecule. Additional data on inhibitors presented herein reveals the importance of two hydrogen-bonding networks toward inhibitory potency: one between Asn131 and an appropriately positioned inhibitor heteroatom and one between a bound water molecule and a second inhibitor heteroatom.
Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site.,Chen JM, Xu SL, Wawrzak Z, Basarab GS, Jordan DB Biochemistry. 1998 Dec 22;37(51):17735-44. PMID:9922139<ref>PMID:9922139</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3std" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 13:07, 14 March 2024

SCYTALONE DEHYDRATASE AND CYANOCINNOLINE INHIBITOR

3std, resolution 1.65Å

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