View source for 5dit


==The Fk1 domain of FKBP51 in complex with the new synthetic ligand (1R)-3-(3,4-dimethoxyphenyl)-1-f3-[2-(morpholin-4-yl)ethoxy]phenylgpropyl(2S)-1-[(2S,3R)-2-cyclohexyl-3-hydroxybutanoyl]piperidine-2-carboxylate==
<StructureSection load='5dit' size='340' side='right'caption='[[5dit]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5dit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DIT 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5B8:(1R)-3-(3,4-DIMETHOXYPHENYL)-1-{3-[2-(MORPHOLIN-4-YL)ETHOXY]PHENYL}PROPYL+(2S)-1-[(2S,3R)-2-CYCLOHEXYL-3-HYDROXYBUTANOYL]PIPERIDINE-2-CARBOXYLATE'>5B8</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=5dit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dit OCA], [https://pdbe.org/5dit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dit RCSB], [https://www.ebi.ac.uk/pdbsum/5dit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dit ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The FK506-binding protein 51 (FKBP51) is a promising drug target for the treatment of stress-related psychiatric or metabolic disorders. Just recently, the first selective ligands for FKBP51 were reported based on an induced fit mechanism, but they are too large for a further drug development process. We therefore designed and synthesized a novel series of selective ligands to explore the requirements necessary for binding to the induced-fit conformation. All ligands of this series show no binding toward the structurally very similar antitarget FKBP52. With the cocrystal structure of the best ligand in this novel series we confirmed the induced fit mechanism. Furthermore, the structure-affinity relationship provides information about beneficial structural features, which is valuable for the development of improved FKBP51-directed drugs.

Structure-Affinity Relationship Analysis of Selective FKBP51 Ligands.,Feng X, Sippel C, Bracher A, Hausch F J Med Chem. 2015 Oct 8;58(19):7796-806. doi: 10.1021/acs.jmedchem.5b00785. Epub, 2015 Sep 30. PMID:26419422<ref>PMID:26419422</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5dit" style="background-color:#fffaf0;"></div>

==See Also==
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bracher A]]
[[Category: Feng X]]
[[Category: Hausch F]]
[[Category: Sippel C]]