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5ics
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of 17beta-hydroxysteroid dehydrogenase type 14 apoenzyme.== | |
| + | <StructureSection load='5ics' size='340' side='right' caption='[[5ics]], [[Resolution|resolution]] 1.52Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ics]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ICS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ICS FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5en4|5en4]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ics FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ics OCA], [http://pdbe.org/5ics PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ics RCSB], [http://www.ebi.ac.uk/pdbsum/5ics PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ics ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DHB14_HUMAN DHB14_HUMAN]] Has NAD-dependent 17-beta-hydroxysteroid dehydrogenase activity. Converts oestradiol to oestrone. The physiological substrate is not known. Acts on oestradiol and 5-androstene-3-beta,17-beta-diol (in vitro).<ref>PMID:17067289</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 17beta-HSD14 is a SDR enzyme able to oxidize estradiol and 5-androstenediol using NAD+. We determined the crystal structure of this human enzyme as the holo form and as ternary complexes with estrone and with the first potent, nonsteroidal inhibitor. The structures reveal a conical, rather large and lipophilic binding site and are the starting point for structure-based inhibitor design. The two natural variants (S205 and T205) were characterized and adopt a similar structure. | ||
| - | + | New Insights into Human 17beta-Hydroxysteroid Dehydrogenase Type 14: First Crystal Structures in Complex with a Steroidal Ligand and with a Potent Nonsteroidal Inhibitor.,Bertoletti N, Braun F, Lepage M, Moller G, Adamski J, Heine A, Klebe G, Marchais-Oberwinkler S J Med Chem. 2016 Jul 12. PMID:27362750<ref>PMID:27362750</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ics" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bertoletti, N]] | [[Category: Bertoletti, N]] | ||
| + | [[Category: Heine, A]] | ||
| + | [[Category: Klebe, G]] | ||
| + | [[Category: Marchais-Oberwinkler, S]] | ||
| + | [[Category: Apoenzyme]] | ||
| + | [[Category: Hydroxysteroid dehydrogenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 11:46, 14 July 2016
Crystal structure of 17beta-hydroxysteroid dehydrogenase type 14 apoenzyme.
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