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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fj2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Curvularia_lunata Curvularia lunata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJ2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fj2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Curvularia_lunata Curvularia lunata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJ2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=QSO:5,7-DIHYDROXY-3-(4-METHOXYPHENYL)-4H-CHROMEN-4-ONE'>QSO</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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=QSO:5,7-DIHYDROXY-3-(4-METHOXYPHENYL)-4H-CHROMEN-4-ONE'>QSO</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=4fj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fj2 OCA], [https://pdbe.org/4fj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4fj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fj2 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=4fj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fj2 OCA], [https://pdbe.org/4fj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4fj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fj2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/O93874_COCLU O93874_COCLU]  
[https://www.uniprot.org/uniprot/O93874_COCLU O93874_COCLU]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phytoestrogens are plant-derived compounds that functionally and structurally mimic mammalian estrogens. Phytoestrogens have broad inhibitory activities toward several steroidogenic enzymes, such as the 17beta-hydroxysteroid dehydrogenases (17beta-HSDs), which modulate the biological potency of androgens and estrogens in mammals. However, to date, no crystallographic data are available to explain phytoestrogens binding to mammalian 17beta-HSDs. NADP(H)-dependent 17beta-HSD from the filamentous fungus Cochliobolus lunatus (17beta-HSDcl) has been the subject of extensive biochemical, kinetic and quantitative structure-activity relationship studies that have shown that the flavonols are the most potent inhibitors. In the present study, we investigated the structure-activity relationships of the ternary complexes between the holo form of 17beta-HSDcl and the flavonols kaempferol and 3,7-dihydroxyflavone, in comparison with the isoflavones genistein and biochanin A. Crystallographic data are accompanied by kinetic analysis of the inhibition mechanisms for six flavonols (3-hydroxyflavone, 3,7-dihydroxyflavone, kaempferol, quercetin, fisetin, myricetin), one flavanone (naringenin), one flavone (luteolin), and two isoflavones (genistein, biochanin A). The kinetics analysis shows that the degree of hydroxylation of ring B significantly influences the overall inhibitory efficacy of the flavonols. A distinct binding mode defines the interactions between 17beta-HSDcl and the flavones and isoflavones. Moreover, the complex with biochanin A reveals an unusual binding mode that appears to account for its greater inhibition of 17beta-HSDcl with respect to genistein. Overall, these data provide a blueprint for identification of the distinct molecular determinants that underpin 17beta-HSD inhibition by phytoestrogens.
Structural basis for inhibition of 17beta-hydroxysteroid dehydrogenases by phytoestrogens: The case of fungal 17beta-HSDcl.,Cassetta A, Stojan J, Krastanova I, Kristan K, Brunskole Svegelj M, Lamba D, Rizner TL J Steroid Biochem Mol Biol. 2017 Jul;171:80-93. doi: 10.1016/j.jsbmb.2017.02.020., Epub 2017 Mar 1. PMID:28259640<ref>PMID:28259640</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4fj2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
== References ==
<references/>
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</StructureSection>
</StructureSection>

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