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| | <StructureSection load='3o5p' size='340' side='right'caption='[[3o5p]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='3o5p' size='340' side='right'caption='[[3o5p]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o5p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5P FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o5p]] 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=3O5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5P FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3o5d|3o5d]], [[3o5e|3o5e]], [[3o5f|3o5f]], [[3o5g|3o5g]], [[3o5i|3o5i]], [[3o5j|3o5j]], [[3o5k|3o5k]], [[3o5l|3o5l]], [[3o5m|3o5m]], [[3o5o|3o5o]], [[3o5q|3o5q]], [[3o5r|3o5r]], [[1kt0|1kt0]]</div></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]] 1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIG6, FKBP5, FKBP51 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5p OCA], [https://pdbe.org/3o5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5p RCSB], [https://www.ebi.ac.uk/pdbsum/3o5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5p 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=3o5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5p OCA], [https://pdbe.org/3o5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5p RCSB], [https://www.ebi.ac.uk/pdbsum/3o5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5p ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN]] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
| + | [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 ==
| + | |
| - | Steroid hormone receptors are key components of mammalian stress and sex hormone systems. Many of them rely on the Hsp90 chaperone system for full function and are further fine-tuned by Hsp90-associated peptidyl-prolyl isomerases such as FK506-binding proteins 51 and 52. FK506-binding protein 51 (FKBP51) has been shown to reduce glucocorticoid receptor signalling and has been genetically associated with human stress resilience and with numerous psychiatric disorders. The peptidyl-prolyl isomerase domain of FKBP51 contains a high-affinity binding site for the natural products FK506 and rapamycin and has further been shown to convey most of the inhibitory activity on the glucocorticoid receptor. FKBP51 has therefore become a prime new target for the treatment of stress-related affective disorders that could be amenable to structure-based drug design. Here, a series of high-resolution structures of the peptidyl-prolyl isomerase domain of FKBP51 as well as a cocrystal structure with the prototypic ligand FK506 are described. These structures provide a detailed picture of the drug-binding domain of FKBP51 and the molecular binding mode of its ligand as a starting point for the rational design of improved inhibitors.
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| - | | + | |
| - | Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.,Bracher A, Kozany C, Thost AK, Hausch F Acta Crystallogr D Biol Crystallogr. 2011 Jun;67(Pt 6):549-59. Epub 2011 May 17. PMID:21636895<ref>PMID:21636895</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3o5p" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| | *[[FKBP 3D structures|FKBP 3D structures]] | | *[[FKBP 3D structures|FKBP 3D structures]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Bracher A]] |
| - | [[Category: Bracher, A]] | + | [[Category: Hausch F]] |
| - | [[Category: Hausch, F]] | + | [[Category: Kozany C]] |
| - | [[Category: Kozany, C]] | + | [[Category: Thost A-K]] |
| - | [[Category: Thost, A K]] | + | |
| - | [[Category: Fk-506 binding domain]]
| + | |
| - | [[Category: Hsp90 cochaperone]]
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| - | [[Category: Immunophiline]]
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| - | [[Category: Isomerase]]
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| - | [[Category: Peptidyl-prolyl isomerase]]
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