4drq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4drq]] 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=4DRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4drq]] 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=4DRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DRQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0OS:{3-[(1S)-1-[({(2S)-1-[(3,5-DICHLOROPHENYL)SULFONYL]PIPERIDIN-2-YL}CARBONYL)OXY]-3-(3,4-DIMETHOXYPHENYL)PROPYL]PHENOXY}ACETIC+ACID'>0OS</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]] 1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0OS:{3-[(1S)-1-[({(2S)-1-[(3,5-DICHLOROPHENYL)SULFONYL]PIPERIDIN-2-YL}CARBONYL)OXY]-3-(3,4-DIMETHOXYPHENYL)PROPYL]PHENOXY}ACETIC+ACID'>0OS</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=4drq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drq OCA], [https://pdbe.org/4drq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drq RCSB], [https://www.ebi.ac.uk/pdbsum/4drq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drq 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=4drq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4drq OCA], [https://pdbe.org/4drq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4drq RCSB], [https://www.ebi.ac.uk/pdbsum/4drq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4drq 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 ==
FK506-binding proteins (FKBP) 51 and 52 are co-chaperones that modulate the signal transduction of steroid hormone receptors. Single nucleotide polymorphisms in the gene encoding FKBP51 have been associated with a variety of psychiatric disorders. Rapamycin and FK506 are two macrocyclic natural products, which tightly bind to all these proteins. A bio-isosteric replacement of the alpha-ketoamide moiety of rapamycin and FK506 with a sulfonamide was envisaged with the retention of the conserved hydrogen bonds. A focused solid support-based synthesis protocol was developed, which led to ligands with submicromolar affinity for FKBP51 and FKBP52. The molecular binding mode for one sulfonamide analog was confirmed by X-ray crystallography.
 
Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52.,Gopalakrishnan R, Kozany C, Wang Y, Schneider S, Hoogeland B, Bracher A, Hausch F J Med Chem. 2012 Mar 29. PMID:22455398<ref>PMID:22455398</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4drq" style="background-color:#fffaf0;"></div>


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

Latest revision as of 17:43, 14 March 2024

Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acidExploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acid

Structural highlights

4drq is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FKBP5_HUMAN Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.

See Also

4drq, resolution 1.00Å

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