3o5d: Difference between revisions
New page: '''Unreleased structure''' The entry 3o5d is ON HOLD Authors: Bracher, A., Kozany, C., Thost, A.-K., Hausch, F. Description: TBA ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] ... |
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==Crystal structure of a fragment of FKBP51 comprising the Fk1 and Fk2 domains== | |||
<StructureSection load='3o5d' size='340' side='right'caption='[[3o5d]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3o5d]] is a 2 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=3O5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5D 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]] 4Å</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=3o5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5d OCA], [https://pdbe.org/3o5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5d RCSB], [https://www.ebi.ac.uk/pdbsum/3o5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5d 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 == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3o5d" 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: Hausch F]] | |||
[[Category: Kozany C]] | |||
[[Category: Thost A-K]] | |||